Entry ID
stringlengths 4
4
| Experimental Method
stringclasses 2
values | Matthews Coefficient
float64 0.41
7.24
⌀ | Percent Solvent Content
float64 0.47
83
⌀ | Crystallization Method
stringclasses 15
values | pH
float64 3
11
⌀ | Crystal Growth Procedure
stringlengths 3
1.23k
⌀ | Temp (K)
float64 273
316
⌀ | Deposition Date
stringdate 2013-04-23 00:00:00
2024-08-20 00:00:00
| Release Date
stringdate 2015-01-07 00:00:00
2024-09-11 00:00:00
| Number of Non-Hydrogen Atoms per Deposited Model
float64 395
50.9k
| Total Number of Polymer Instances (Chains)
float64 1
42
| Total Number of Polymer Residues per Deposited Model
float64 39
6.96k
| Number of Water Molecules per Deposited Model
float64 1
3.43k
⌀ | Disulfide Bond Count per Deposited Model
float64 1
73
⌀ | Molecular Weight per Deposited Model
float64 4.98
778
| Number of Distinct Protein Entities
float64 1
15
| Refinement Resolution (Å)
stringlengths 1
13
| Structure Determination Methodology
stringclasses 1
value | Average B Factor
float64 6.66
145
⌀ | R Free
float64 0.12
0.38
⌀ | R Work
float64 0.1
0.32
⌀ | Structure Title
stringlengths 7
292
| Sequence
stringlengths 3
2.13k
| Entity Polymer Type
stringclasses 3
values | Polymer Entity Sequence Length
float64 3
2.13k
| Entity Macromolecule Type
stringclasses 4
values | Total Number of polymer Entity Instances (Chains) per Entity
float64 1
12
| Molecular Weight (Entity)
float64 0.23
241
| Macromolecule Name
stringlengths 3
299
| EC Number
stringclasses 444
values | EC Provenance Source
stringclasses 1
value | Source Organism
stringclasses 76
values | Taxonomy ID
float64 274
3.05M
| Total Number of Polymer Residues per Assembly
float64 23
6.96k
| Total Number of Polymer Instances (Chains) per Assembly
float64 1
34
| Oligomeric Count
float64 1
34
| Assembly ID
float64 1
1
| Oligomeric State
stringclasses 20
values | Stoichiometry
stringclasses 38
values | Ligand ID
stringlengths 1
5
⌀ | Ligand Formula
stringlengths 1
22
⌀ | Ligand MW
float64 16
1.77k
⌀ | Ligand Name
stringlengths 4
573
⌀ | InChI
stringlengths 14
556
⌀ | Ligand SMILES
stringlengths 1
207
⌀ | Ligand of Interest
stringclasses 1
value | __index_level_0__
int64 1
11.8k
|
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
7CMB
|
X-RAY DIFFRACTION
| 2.78
| 55.78
|
VAPOR DIFFUSION
| 8.5
|
0.2M Ammonium sulfate, 0.1M Tris pH 8.5, 25% PEG3350
| 291
|
2020-07-26
|
2021-07-28
| 2,333
| 1
| 293
| 4
| null | 33.47
| 1
|
2.592
|
experimental
| 75.003
| 0.2509
| 0.2059
|
Crystal Structure of PAK4 in complex with inhibitor 41
|
SSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
|
Protein
| 293
|
polypeptide(L)
| 1
| 33.098
|
Serine/threonine-protein kinase PAK 4
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 293
| 1
| 1
| 1
|
Monomer
|
A1
|
G5X
|
C21 H21 N5 O2
| 375.424
|
1-(2-azanylpyrimidin-4-yl)-6-[2-(1-oxidanylcyclohexyl)ethynyl]indole-3-carboxamide
|
InChI=1S/C21H21N5O2/c22-19(27)16-13-26(18-7-11-24-20(23)25-18)17-12-14(4-5-15(16)17)6-10-21(28)8-2-1-3-9-21/h4-5,7,11-13,28H,1-3,8-9H2,(H2,22,27)(H2,23,24,25)
|
c1cc2c(cc1C#CC3(CCCCC3)O)n(cc2C(=O)N)c4ccnc(n4)N
|
Y
| 2,865
|
5CTP
|
X-RAY DIFFRACTION
| 2.25
| 45.44
|
VAPOR DIFFUSION, HANGING DROP
| 6.5
|
107mM Mes pH 6.5, 29% glycerol ethoxylate, 1 M ammonium acetate
| 298
|
2015-07-24
|
2016-11-30
| 5,831
| 2
| 704
| 212
| null | 83.9
| 1
|
2.033
|
experimental
| 56.12
| 0.1989
| 0.1848
|
Crystal structure of CK2alpha with N-(3-(3-chloro-4-(phenyl)benzylamino)propyl)acetamide bound
|
GSMDIEFDDDADDDGSGSGSGSGSSGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVKKKKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVK
|
Protein
| 352
|
polypeptide(L)
| 2
| 41.468
|
Casein kinase II subunit alpha
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 352
| 1
| 1
| 1
|
Monomer
|
A1
|
ACT
|
C2 H3 O2
| 59.044
|
ACETATE ION
|
InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
|
CC(=O)[O-]
| null | 3,721
|
6L5N
|
X-RAY DIFFRACTION
| 2.6
| 52.74
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
7% MPD and 0.1M Bicine, pH8.5
| 293
|
2019-10-24
|
2020-06-17
| 6,518
| 4
| 784
| 156
| null | 95.63
| 1
|
2.242
|
experimental
| 37.7253
| 0.233
| 0.1753
|
Crystal structure of human DEAD-box RNA helicase DDX21 at post-unwound state
|
SFSNFPISEETIKLLKGRGVTFLFPIQAKTFHHVYSGKDLIAQARTGTGKTFSFAIPLIEKLHGELQDRKRGRAPQVLVLAPTRELANQVSKDFSDITKKLSVACFYGGTPYGGQFERMRNGIDILVGTPGRIKDHIQNGKLDLTKLKHVVLDEVDQMLDMGFADQVEEILSVAYKKDSEDNPQTLLFSATCPHWVFNVAKKYMKSTYEQVDLIGKKTQKTAITVEHLAIKCHWTQRAAVIGDVIRVYSGHQGRTIIFCETKKEAQELSQNSAIKQDAQSLHGDIPQKQREITLKGFRNGSFGVLVATNVAARGLDIPEVDLVIQSSPPKDVESYIHRSGRTGRAGRTGVCICFYQHKEEYQLVQVEQKAGIKFKRI
|
Protein
| 377
|
polypeptide(L)
| 2
| 42.471
|
Nucleolar RNA helicase 2
|
3.6.4.13
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 392
| 2
| 2
| 1
|
Monomer
|
A1
|
ANP
|
C10 H17 N6 O12 P3
| 506.196
|
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER
|
InChI=1S/C10H17N6O12P3/c11-8-5-9(13-2-12-8)16(3-14-5)10-7(18)6(17)4(27-10)1-26-31(24,25)28-30(22,23)15-29(19,20)21/h2-4,6-7,10,17-18H,1H2,(H,24,25)(H2,11,12,13)(H4,15,19,20,21,22,23)/t4-,6-,7-,10-/m1/s1
|
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(NP(=O)(O)O)O)O)O)N
|
Y
| 6,377
|
6VNY
|
X-RAY DIFFRACTION
| 1.85
| 33.64
|
EVAPORATION
| 8
|
0.1 M bis-tris pH 5.5, 0.25 M NaCl, 10 mM TCEP, 27-33% PEG-3350
| 298
|
2020-01-29
|
2020-04-08
| 2,470
| 1
| 318
| 131
| null | 36.94
| 1
|
2.3
|
experimental
| 40.75
| 0.2292
| 0.1736
|
Crystal structure of TYK2 kinase with compound 10
|
MAHHHHHHHHHHGALEVLFQGPGDPTVFHKRYLKKIRDLGEGHFGKVSLYCYDPTNDGTGEMVAVKALKADAGPQHRSGWKQEIDILRTLYHEHIIKYKGCCEDAGAASLQLVMEYVPLGSLRDYLPRHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTKFLELIGIAQGQMTVLRLTELLERGERLPRPDKCPAEVYHLMKNCWETEASFRPTFENLIPILKTVHEKYQGQAPS
|
Protein
| 318
|
polypeptide(L)
| 1
| 36.551
|
Non-receptor tyrosine-protein kinase TYK2
|
2.7.10.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 318
| 1
| 1
| 1
|
Monomer
|
A1
|
R4S
|
C18 H22 F N7 O2
| 387.411
|
N-[(1S,5R)-3-(5-fluoro-2-{[1-(2-hydroxyethyl)-1H-pyrazol-4-yl]amino}pyrimidin-4-yl)-3-azabicyclo[3.1.0]hexan-1-yl]cyclopropanecarboxamide
|
InChI=1S/C18H22FN7O2/c19-14-7-20-17(22-13-6-21-26(9-13)3-4-27)23-15(14)25-8-12-5-18(12,10-25)24-16(28)11-1-2-11/h6-7,9,11-12,27H,1-5,8,10H2,(H,24,28)(H,20,22,23)/t12-,18-/m1/s1
|
c1c(cn(n1)CCO)Nc2ncc(c(n2)N3CC4CC4(C3)NC(=O)C5CC5)F
|
Y
| 2,291
|
6WBW
|
X-RAY DIFFRACTION
| 2.43
| 49.43
|
VAPOR DIFFUSION, HANGING DROP
| null |
25% PEG 3350, 0.2 M ammonium sulfate, 0.1 M Hepes pH 7.5
| 293
|
2020-03-27
|
2020-05-06
| 10,250
| 3
| 1,128
| 1,121
| null | 131.75
| 1
|
1.46
|
experimental
| 26.28
| 0.197
| 0.172
|
Structure of Human HDAC2 in complex with an ethyl ketone inhibitor
|
MAYSQGGGKKKVCYYYDGDIGNYYYGQGHPMKPHRIRMTHNLLLNYGLYRKMEIYRPHKATAEEMTKYHSDEYIKFLRSIRPDNMSEYSKQMQRFNVGEDCPVFDGLFEFCQLSTGGSVAGAVKLNRQQTDMAVNWAGGLHHAKKSEASGFCYVNDIVLAILELLKYHQRVLYIDIDIHHGDGVEEAFYTTDRVMTVSFHKYGEYFPGTGDLRDIGAGKGKYYAVNFPMRDGIDDESYGQIFKPIISKVMEMYQPSAVVLQCGADSLSGDRLGCFNLTVKGHAKCVEVVKTFNLPLLMLGGGGYTIRNVARCWTYETAVALDCEIPNELPYNDYFEYFGPDFKLHISPSNMTNQNTPEYMEKIKQRLFENLRMLPH
|
Protein
| 376
|
polypeptide(L)
| 3
| 43.062
|
Histone deacetylase 2
|
3.5.1.98
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 376
| 1
| 1
| 1
|
Monomer
|
A1
|
TV1
|
C27 H37 N5 O4
| 495.614
|
N-{(1S)-7,7-dihydroxy-1-[5-(2-methoxyquinolin-3-yl)-1H-imidazol-2-yl]nonyl}-1-methylazetidine-3-carboxamide
|
InChI=1S/C27H37N5O4/c1-4-27(34,35)13-9-5-6-12-22(30-25(33)19-16-32(2)17-19)24-28-15-23(29-24)20-14-18-10-7-8-11-21(18)31-26(20)36-3/h7-8,10-11,14-15,19,22,34-35H,4-6,9,12-13,16-17H2,1-3H3,(H,28,29)(H,30,33)/t22-/m0/s1
|
CCC(CCCCCC(c1[nH]c(cn1)c2cc3ccccc3nc2OC)NC(=O)C4CN(C4)C)(O)O
|
Y
| 10,190
|
4Z6F
|
X-RAY DIFFRACTION
| 2.25
| 45.34
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
14% to 23% PEG3400, and 350 mM sodium acetate in 50 mM imidazole (pH 7.5)
| 298
|
2015-04-04
|
2016-04-13
| 3,350
| 4
| 366
| 79
| null | 48.31
| 1
|
2.444
|
experimental
| null | 0.2483
| 0.1949
|
Structure of human DNA polymerase beta 279NA mutant complexed with G in the template base paired with incoming non-hydrolyzable TTP and MANGANESE
|
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFAKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
|
Protein
| 335
|
polypeptide(L)
| 1
| 38.199
|
DNA polymerase beta
|
2.7.7.7
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 366
| 4
| 4
| 1
|
Monomer
|
A1
|
MN
|
Mn
| 54.938
|
MANGANESE (II) ION
|
InChI=1S/Mn/q+2
|
[Mn+2]
| null | 83
|
4QMV
|
X-RAY DIFFRACTION
| 2.55
| 51.71
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
12.5 mg/mL MST3, 1 mM PF-03814735, 25 mM TRIS, PH 8.0, 50 MM HEPES pH 7.5, 125 mM SODIUM CHLORIDE, 100 mM MAGNESIUM CHLORIDE, 15% PEG 400, VAPOR DIFFUSION, HANGING DROP, temperature 291K
| 291
|
2014-06-16
|
2015-07-01
| 2,448
| 1
| 310
| 91
| null | 35.62
| 1
|
2.4
|
experimental
| null | 0.2264
| 0.1674
|
MST3 IN COMPLEX WITH PF-03814735, N-{2-[(1S,4R)-6-{[4-(CYCLOBUTYLAMINO)-5-(TRIFLUOROMETHYL)PYRIMIDIN-2-YL]AMINO}-1,2,3,4-TETRAHYDRO-1,4-EPIMINONAPHTHALEN-9-YL]-2-OXOETHYL}ACETAMIDE
|
GPLGSEFMAHSPVQSGLPGMQNLKADPEELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSALDLLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPPHSELHPMKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTAKELLKHKFILRNAKKTSYLTELIDRYKRWKAEQSHDDS
|
Protein
| 310
|
polypeptide(L)
| 1
| 35.024
|
SERINE/THREONINE-PROTEIN KINASE 24
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 310
| 1
| 1
| 1
|
Monomer
|
A1
|
34W
|
C23 H25 F3 N6 O2
| 474.479
|
N-{2-[(1S,4R)-6-{[4-(cyclobutylamino)-5-(trifluoromethyl)pyrimidin-2-yl]amino}-1,2,3,4-tetrahydro-1,4-epiminonaphthalen-9-yl]-2-oxoethyl}acetamide
|
InChI=1S/C23H25F3N6O2/c1-12(33)27-11-20(34)32-18-7-8-19(32)16-9-14(5-6-15(16)18)30-22-28-10-17(23(24,25)26)21(31-22)29-13-3-2-4-13/h5-6,9-10,13,18-19H,2-4,7-8,11H2,1H3,(H,27,33)(H2,28,29,30,31)/t18-,19+/m0/s1
|
CC(=O)NCC(=O)N1C2CCC1c3c2ccc(c3)Nc4ncc(c(n4)NC5CCC5)C(F)(F)F
| null | 5,146
|
7V8F
|
X-RAY DIFFRACTION
| 1.98
| 36.94
|
EVAPORATION
| 8
|
2%(v/v) 1,4-dioxane, 0.1 M Tris-HCl (pH 8.0), 15%(w/v) PEG 3,350.
| 289
|
2021-08-22
|
2022-03-30
| 2,160
| 2
| 261
| 192
| null | 29.96
| 2
|
1.66
|
experimental
| 30.76
| 0.198
| 0.1753
|
Crystal structure of UBE2L3 bound to HOIP RING1 domain.
|
GPGSEFQECAVCGWALPHNRMQALTSCECTICPDCFRQHFTIALKEKHITDMVCPACGRPDLTDDTQLLSYFSTLDIQLRESLEPDAYALFHKKLTEGVLMRD
|
Protein
| 103
|
polypeptide(L)
| 1
| 11.637
|
E3 ubiquitin-protein ligase RNF31
|
2.3.2.31
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 261
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 6,984
|
5R5E
|
X-RAY DIFFRACTION
| 2.02
| 39
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
0.1M HEPES pH 7.5, 0.3M sodium/potassium phosphate, 15% PEG Smear High, 20% ethylene glycol
| 277
|
2020-02-28
|
2020-07-01
| 2,444
| 1
| 304
| 161
| null | 33.23
| 1
|
1.58
|
experimental
| 26.243
| 0.2245
| 0.1888
|
PanDDA analysis group deposition -- Crystal Structure of human NUDT22 in complex with N13848a
|
SMDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVRRLPETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL
|
Protein
| 304
|
polypeptide(L)
| 1
| 32.707
|
Uridine diphosphate glucose pyrophosphatase NUDT22
|
3.6.1.45
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 304
| 1
| 1
| 1
|
Monomer
|
A1
|
GV1
|
C10 H13 N3 S
| 207.295
|
~{N},~{N},5,6-tetramethylthieno[2,3-d]pyrimidin-4-amine
|
InChI=1S/C10H13N3S/c1-6-7(2)14-10-8(6)9(13(3)4)11-5-12-10/h5H,1-4H3
|
Cc1c(sc2c1c(ncn2)N(C)C)C
| null | 1,945
|
9FLT
|
X-RAY DIFFRACTION
| 3.16
| 61.01
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
45% MPD
0.1M SPG 6.5
| 278
|
2024-06-05
|
2024-09-11
| 2,643
| 1
| 336
| 66
| null | 38.62
| 1
|
2.4
|
experimental
| 54.563
| 0.23881
| 0.18392
|
Crystal structure of human Haspin (GSG2) kinase bound to chemical probe MU1920
|
SMGECSQKGPVPFSHCLPTEKLQRCEKIGEGVFGEVFQTIADHTPVAIKIIAIEGPDLVNGSHQKTFEEILPEIIISKELSLLSGEVCNRTEGFIGLNSVHCVQGSYPPLLLKAWDHYNSTKGSANDRPDFFKDDQLFIVLEFEFGGIDLEQMRTKLSSLATAKSILHQLTASLAVAEASLRFEHRDLHWGNVLLKKTSLKKLHYTLNGKSSTIPSCGLQVSIIDYTLSRLERDGIVVFCDVSMDEDLFTGDGDYQFDIYRLMKKENNNRWGEYHPYSNVLWLHYLTDKMLKQMTFKTKCNTPAMKQIKRKIQEFHRTMLNFSSATDLLCQHSLFK
|
Protein
| 336
|
polypeptide(L)
| 1
| 38.24
|
Serine/threonine-protein kinase haspin
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 336
| 1
| 1
| 1
|
Monomer
|
A1
|
A1IDF
|
C17 H15 N5 S
| 321.4
|
~{N}-(1,4-dimethylpyrazol-3-yl)-3-pyridin-4-yl-thieno[3,2-b]pyridin-5-amine
|
InChI=1S/C17H15N5S/c1-11-9-22(2)21-17(11)20-15-4-3-14-16(19-15)13(10-23-14)12-5-7-18-8-6-12/h3-10H,1-2H3,(H,19,20,21)
|
Cc1cn(nc1Nc2ccc3c(n2)c(cs3)c4ccncc4)C
|
Y
| 1,649
|
5T53
|
X-RAY DIFFRACTION
| 3.89
| 68.37
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
8% PEG 8000, 0.1M HEPES, pH 7.5 and 10 % ethylene glycol
| 298.15
|
2016-08-30
|
2016-11-09
| 1,436
| 1
| 227
| 14
| null | 27.12
| 1
|
2.699
|
experimental
| null | 0.2852
| 0.2496
|
MOLECULAR BASIS FOR COHESIN ACETYLATION BY ESTABLISHMENT OF SISTER CHROMATID COHESION N-ACETYLTRANSFERASE ESCO1
|
KTDEKQLIIDAGQKRFGAVSCNVCGMLYTASNPEDETQHLLFHNQFISAVKYVGWKKERILAEYPDGRIIMVLPEDPKYALKKVDEIREMVDNDLGFQQAPLMCYSRTKTLLFISNDKKVVGCLIAEHIQWGYRVIEEKLPVIRSEEEKVRFERQKAWCCSTLPEPAICGISRIWVFSMMRRKKIASRMIECLRSNFIYGSYLSKEEIAFSDPTPDGKLFATQYCGT
|
Protein
| 227
|
polypeptide(L)
| 1
| 26.248
|
N-acetyltransferase ESCO1
|
2.3.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 227
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 4,176
|
6Q7K
|
X-RAY DIFFRACTION
| 2.28
| 45.95
|
VAPOR DIFFUSION, SITTING DROP
| 7.2
|
0.2M (NH4)2SO4
33% MPEG 2000
0.02M Mercaptoethanol
0.1M pH=7.2 HEPES/NaOH
| 293
|
2018-12-13
|
2019-03-27
| 3,103
| 1
| 368
| 284
| null | 42.73
| 1
|
1.84
|
experimental
| 34.718
| 0.26315
| 0.21091
|
ERK2 mini-fragment binding
|
MAHHHHHHMAAAAAAGAGPEMVRGQVFDVGPRYTNLSYIGEGAYGMVCSAYDNVNKVRVAIKKISPFEHQTYCQRTLREIKILLRFRHENIIGINDIIRAPTIEQMKDVYIVQDLMETDLYKLLKTQHLSNDHICYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTTCDLKICDFGLARVADPDHDHTGFLTEYVATRWYRAPEIMLNSKGYTKSIDIWSVGCILAEMLSNRPIFPGKHYLDQLNHILGILGSPSQEDLNCIINLKARNYLLSLPHKNKVPWNRLFPNADSKALDLLDKMLTFNPHKRIEVEQALAHPYLEQYYDPSDEPIAEAPFKFDMELDDLPKEKLKELIFEETARFQPGYRS
|
Protein
| 368
|
polypeptide(L)
| 1
| 42.552
|
Mitogen-activated protein kinase 1
|
2.7.11.24
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 368
| 1
| 1
| 1
|
Monomer
|
A1
|
SO4
|
O4 S
| 96.063
|
SULFATE ION
|
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
|
[O-]S(=O)(=O)[O-]
| null | 10,656
|
8SLU
|
X-RAY DIFFRACTION
| 2.56
| 52.01
|
VAPOR DIFFUSION, SITTING DROP
| 5.65
|
30% PEG 3350, 200 mM Li2SO4, 100 mM bis-tris pH 5.65
| 293.15
|
2023-04-24
|
2023-06-21
| 2,547
| 1
| 282
| 98
| null | 32.8
| 1
|
1.84
|
experimental
| 41.64
| 0.2366
| 0.1948
|
Crystal structure of human STEP (PTPN5) at cryogenic temperature (100 K) and high pressure (205 MPa)
|
SMSRVLQAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLSH
|
Protein
| 282
|
polypeptide(L)
| 1
| 32.518
|
Tyrosine-protein phosphatase non-receptor type 5
|
3.1.3.48
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 282
| 1
| 1
| 1
|
Monomer
|
A1
|
SO4
|
O4 S
| 96.063
|
SULFATE ION
|
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
|
[O-]S(=O)(=O)[O-]
| null | 2,724
|
6GUU
|
X-RAY DIFFRACTION
| 3.8
| 67.61
|
VAPOR DIFFUSION, HANGING DROP
| null |
0.2 M ammonium nitrate
20 % PEG 3350
2 % benzamidine hydrochloride
| 277
|
2018-06-19
|
2019-10-09
| 3,394
| 2
| 482
| null | null | 57.43
| 1
|
2.95
|
experimental
| 117.22
| 0.263
| 0.2063
|
Structure of CHD5 PHD2 - tandem chromodomains
|
GPGEDDHMEFCRVCKDGGELLCCDACPSSYHLHCLNPPLPEIPNGEWLCPRCTCPPLKGKVQRILHWRWTEPPAPFMVGLPGPDVEPSLPPPKPLEGIPEREFFVKWAGLSYWHCSWVKELQLELYHTVMYRNYQRKNDMDEPPPFDYGSGDEDGKSEKRKNKDPLYAKMEERFYRYGIKPEWMMIHRILNHSFDKKGDVHYLIKWKDLPYDQCTWEIDDIDIPYYDNLKQAYWGHRELML
|
Protein
| 241
|
polypeptide(L)
| 2
| 28.586
|
Chromodomain-helicase-DNA-binding protein 5
|
3.6.4.12
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 241
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 6,725
|
6WTN
|
X-RAY DIFFRACTION
| 2.09
| 41.16
|
VAPOR DIFFUSION, HANGING DROP
| 5
|
1.6-2.4 M sodium malonate, pH 5
| 291
|
2020-05-03
|
2021-05-05
| 2,416
| 1
| 309
| 93
| null | 36.9
| 1
|
1.83
|
experimental
| 41.6108
| 0.2084
| 0.1872
|
Human JAK2 JH1 domain in complex with Ruxolitinib
|
MAFEDRDPTQFEERHLKFLQQLGKGNFGSVEMCRYDPLQDNTGEVVAVKKLQHSTEEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLKLIMEYLPYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSKSPPAEFMRMIGNDKQGQMIVFHLIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQIRDNMAGGSGSENLYFQ
|
Protein
| 309
|
polypeptide(L)
| 1
| 36.412
|
Tyrosine-protein kinase JAK2
|
2.7.10.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 309
| 1
| 1
| 1
|
Monomer
|
A1
|
EDO
|
C2 H6 O2
| 62.068
|
1,2-ETHANEDIOL
|
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
|
C(CO)O
| null | 10,132
|
7RBH
|
X-RAY DIFFRACTION
| 2.24
| 45.15
|
VAPOR DIFFUSION, HANGING DROP
| 5.5
|
0.1 M Citrate pH 5.5, 18% PEG6000
| 298
|
2021-07-06
|
2022-03-09
| 3,646
| 4
| 372
| 288
| null | 49.89
| 1
|
1.75
|
experimental
| 32.189
| 0.2245
| 0.1793
|
Human DNA polymerase beta crosslinked ternary complex 2
|
GCTGATGCGC
|
DNA
| 10
|
polydeoxyribonucleotide
| 1
| 3.061
|
DNA (5'-D(*GP*CP*TP*GP*AP*TP*GP*CP*GP*C)-3')
| null | null |
synthetic construct
| 32,630
| 372
| 4
| 4
| 1
|
Monomer
|
A1
|
QPJ
|
C5 H14 O10 P2
| 296.106
|
2-deoxy-3,5-di-O-phosphono-D-erythro-pentitol
|
InChI=1S/C5H14O10P2/c6-2-1-5(15-17(11,12)13)4(7)3-14-16(8,9)10/h4-7H,1-3H2,(H2,8,9,10)(H2,11,12,13)/t4-,5+/m1/s1
|
C(CO)C(C(COP(=O)(O)O)O)OP(=O)(O)O
|
Y
| 414
|
7XMK
|
X-RAY DIFFRACTION
| 2.35
| 47.67
|
VAPOR DIFFUSION, HANGING DROP
| null |
0.25M ammonium iodide, 0.03M glycyl-glycyl-glycine, 23% polyethylene glycol (PEG) 3350
| 277
|
2022-04-26
|
2023-04-26
| 4,333
| 2
| 588
| 141
| null | 68.18
| 1
|
2.376
|
experimental
| 39.648
| 0.2585
| 0.2243
|
Crystal structure of human RIPK1 kinase domain in complex with compound SKLB923
|
MQPDMSLNVIKMKSSDFLESAELDSGGFGKVSLAFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIAEQQLIMAIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQLE
|
Protein
| 294
|
polypeptide(L)
| 2
| 33.469
|
Receptor-interacting serine/threonine-protein kinase 1
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 588
| 2
| 2
| 1
|
Homo 2-mer
|
A2
|
IOD
|
I
| 126.904
|
IODIDE ION
|
InChI=1S/HI/h1H/p-1
|
[I-]
| null | 11,238
|
8AWK
|
X-RAY DIFFRACTION
| 2.45
| 49.81
|
VAPOR DIFFUSION, SITTING DROP
| 7
|
0.2 M Na2SO4, 14% (v/v) PEG3350, 0.25 M HEPES pH 7.0
| 293
|
2022-08-30
|
2024-03-13
| 4,872
| 1
| 497
| 547
| 2
| 58.61
| 1
|
1.58
|
experimental
| 19.369
| 0.1849
| 0.1515
|
Structure of recombinant human beta-glucocerebrosidase in complex with D-carbaxylosyl chloride
|
ARPCIPKSFGYSSVVCVCNATYCDSFDPPTFPALGTFSRYESTRSGRRMELSMGPIQANHTGTGLLLTLQPEQKFQKVKGFGGAMTDAAALNILALSPPAQNLLLKSYFSEEGIGYNIIRVPMASCDFSIRTYTYADTPDDFQLHNFSLPEEDTKLKIPLIHRALQLAQRPVSLLASPWTSPTWLKTNGAVNGKGSLKGQPGDIYHQTWARYFVKFLDAYAEHKLQFWAVTAENEPSAGLLSGYPFQCLGFTPEHQRDFIARDLGPTLANSTHHNVRLLMLDDQRLLLPHWAKVVLTDPEAAKYVHGIAVHWYLDFLAPAKATLGETHRLFPNTMLFASEACVGSKFWEQSVRLGSWDRGMQYSHSIITNLLYHVVGWTDWNLALNPEGGPNWVRNFVDSPIIVDITKDTFYKQPMFYHLGHFSKFIPEGSQRVGLVASQKNDLDAVALMHPDGSAVVVVLNRSSKDVPLTIKDPAVGFLETISPGYSIHTYLWRRQ
|
Protein
| 497
|
polypeptide(L)
| 1
| 55.659
|
Lysosomal acid glucosylceramidase
|
3.2.1.45
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 497
| 1
| 1
| 1
|
Monomer
|
A1
|
SO4
|
O4 S
| 96.063
|
SULFATE ION
|
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
|
[O-]S(=O)(=O)[O-]
| null | 2,450
|
6C90
|
X-RAY DIFFRACTION
| 3.59
| 65.72
|
VAPOR DIFFUSION, HANGING DROP
| null |
1.6 M sodium-potassium (L)-tartrate, 0.1 M Bis-Tris pH 6.5
| 291
|
2018-01-25
|
2018-05-30
| 6,228
| 2
| 786
| 238
| null | 90.11
| 2
|
2.2
|
experimental
| null | 0.2214
| 0.1903
|
Human Mtr4 helicase in complex with ZCCHC8-CTD
|
SGDTDEPIFGKKPRIEESITEDLSLADLMPRVKVQSVETVEGCTHEVALPAEEDYLPLKPRVGKAAKEYPFILDAFQREAIQCVDNNQSVLVSAHTSAGKTVCAEYAIALALREKQRVIFTSPIKALSNQKYREMYEEFQDVGLMTGDVTINPTASCLVMTTEILRSMLYRGSEVMREVAWVIFDEIHYMRDSERGVVWEETIILLPDNVHYVFLSATIPNARQFAEWICHLHKQPCHVIYTDYRPTPLQHYIFPAGGDGLHLVVDENGDFREDNFNTAMQVLRDAGDLAKGDQKGRKGGTKGPSNVFKIVKMIMERNFQPVIIFSFSKKDCEAYALQMTKLDFNTDEEKKMVEEVFSNAIDCLSDEDKKLPQVEHVLPLLKRGIGIHHGGLLPILKETIEILFSEGLIKALFATETFAMGINMPARTVLFTNARKFDGKDFRWISSGEYIQMSGRAGRRGMDDRGIVILMVDEKMSPTIGKQLLKGSADPLNSAFHLTYNMVLNLLRVEEINPEYMLEKSFYQFQHYRAIPGSRTVLQMDELKCRKRVLRRLGFATSSDVIEMKGRVACEISSADELLLTEMMFNGLFNDLSAEQATALLSCFVFQENSSEMPKLTEQLAGPLRQMQECAKRIAKVSAEAKLEIDEETYLSSFKPHLMDVVYTWATGATFAHICKMTDVFEGSIIRCMRRLEELLRQMCQAAKAIGNTELENKFAEGITKIKRDIVFAASLYL
|
Protein
| 734
|
polypeptide(L)
| 1
| 83.206
|
Exosome RNA helicase MTR4,Exosome RNA helicase MTR4
|
3.6.4.13
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 786
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
TLA
|
C4 H6 O6
| 150.087
|
L(+)-TARTARIC ACID
|
InChI=1S/C4H6O6/c5-1(3(7)8)2(6)4(9)10/h1-2,5-6H,(H,7,8)(H,9,10)/t1-,2-/m1/s1
|
C(C(C(=O)O)O)(C(=O)O)O
| null | 6,533
|
5MJ6
|
X-RAY DIFFRACTION
| 2.39
| 58.98
|
VAPOR DIFFUSION, SITTING DROP
| 8.5
|
18.8% (w/v) PEG of mean MW 20000, 37.6% (v/v) PEG monomethyl ether of mean MW 500, 50.2 mM Bicine, 43.8 mM Trizma base (pH of buffer mixture: 8.5) and 0.282 M each of the following halogens: Sodium fluoride, Sodium bromide and Sodium iodide
| 291
|
2016-11-30
|
2017-04-05
| 15,376
| 2
| 1,762
| 240
| 2
| 217.25
| 1
|
2.53
|
experimental
| null | 0.2292
| 0.1738
|
Ligand-induced conformational change of Insulin-regulated aminopeptidase: insights on catalytic mechanism and active site plasticity.
|
ATNGKLFPWAQIRLPTAVVPLRYELSLHPNLTSMTFRGSVTISVQALQVTWNIILHSTGHNISRVTFMSAVSSQEKQAEILEYAYHGQIAIVAPEALLAGHNYTLKIEYSANISSSYYGFYGFSYTDESNEKKYFAATQFEPLAARSAFPCFDEPAFKATFIIKIIRDEQYTALSNMPKKSSVVLDDGLVQDEFSESVKMSTYLVAFIVGEMKNLSQDVNGTLVSIYAVPEKIGQVHYALETTVKLLEFFQNYFEIQYPLKKLDLVAIPDFEAGAMENWGLLTFREETLLYDSNTSSMADRKLVTKIIAHELAHQWFGNLVTMKWWNDLWLNEGFATFMEYFSLEKIFKELSSYEDFLDARFKTMKKDSLNSSHPISSSVQSSEQIEEMFDSLSYFKGSSLLLMLKTYLSEDVFQHAVVLYLHNHSYASIQSDDLWDSFNEVTNQTLDVKRMMKTWTLQKGFPLVTVQKKGKELFIQQERFFLNMKPEIQPSDTSYLWHIPLSYVTEGRNYSKYQSVSLLDKKSGVINLTEEVLWVKVNINMNGYYIVHYADDDWEALIHQLKINPYVLSDKDRANLINNIFELAGLGKVPLKRAFDLINYLGNENHTAPITEALFQTDLIYNLLEKLGYMDLASRLVTRVFKLLQNQIQQQTWTDEGTPSMRELRSALLEFACTHNLGNCSTTAMKLFDDWMASNGTQSLPTDVMTTVFKVGAKTDKGWSFLLGKYISIGSEAEKNKILEALASSEDVRKLYWLMKSSLNGDNFRTQKLSFIIRTVGRHFPGHLLAWDFVKENWNKLVQKFPLGSYTIQNIVAGSTYLFSTKTHLSEVQAFFENQSEATFRLRCVQEALEVIQLNIQWMEKNLKSLTWWLRTETSQVAPA
|
Protein
| 881
|
polypeptide(L)
| 2
| 101.182
|
Leucyl-cystinyl aminopeptidase
|
3.4.11.3
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 881
| 1
| 1
| 1
|
Monomer
|
A1
|
NAG
|
C8 H15 N O6
| 221.208
|
2-acetamido-2-deoxy-beta-D-glucopyranose
|
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
|
CC(=O)NC1C(C(C(OC1O)CO)O)O
| null | 7,663
|
6EPU
|
X-RAY DIFFRACTION
| 4.06
| 69.68
|
VAPOR DIFFUSION, HANGING DROP
| 5.5
|
2M (NH4)2SO4, 0.1M Bis-Tris pH 5.5
| 277
|
2017-10-12
|
2018-10-31
| 1,240
| 1
| 130
| 139
| null | 15.8
| 1
|
1.8
|
experimental
| null | 0.2184
| 0.192
|
The ATAD2 bromodomain in complex with compound 2
|
SMQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESR
|
Protein
| 130
|
polypeptide(L)
| 1
| 15.454
|
ATPase family AAA domain-containing protein 2
|
3.6.1.3
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 130
| 1
| 1
| 1
|
Monomer
|
A1
|
SO4
|
O4 S
| 96.063
|
SULFATE ION
|
InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
|
[O-]S(=O)(=O)[O-]
| null | 9,033
|
6O47
|
X-RAY DIFFRACTION
| 2.87
| 57.19
|
VAPOR DIFFUSION, HANGING DROP
| 7
|
0.064 M sodium citrate 7.0, 0.1 M HEPES, pH 7.0, 10% PEG5000MME
| 293
|
2019-02-28
|
2019-05-29
| 3,117
| 1
| 372
| 180
| null | 44.77
| 1
|
2.196
|
experimental
| null | 0.2214
| 0.1815
|
human cGAS core domain (K427E/K428E) bound with RU-521
|
SILVRRDAAPGASKLRAVLEKLKLSRDDISTAAGMVKGVVDHLLLRLKCDSAFRGVGLLNTGSYYEHVKISAPNEFDVMFKLEVPRIQLEEYSNTRAYYFVKFKRNPKENPLSQFLEGEILSASKMLSKFRKIIKEEINDIKDTDVIMKRKRGGSPAVTLLISEKISVDITLALESKSSWPASTQEGLRIQNWLSAKVRKQLRLKPFYLVPKHAKEGNGFQEETWRLSFSHIEKEILNNHGKSKTCCENKEEKCCRKDCLKLMKYLLEQLKERFKDEEHLDKFSSYHVKTAFFHVCTQNPQDSQWDRKDLGLCFDNCVTYFLQCLRTEKLENYFIPEFNLFSSNLIDKRSKEFLTKQIEYERNNEFPVFDEF
|
Protein
| 372
|
polypeptide(L)
| 1
| 43.486
|
Cyclic GMP-AMP synthase
|
2.7.7.86
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 372
| 1
| 1
| 1
|
Monomer
|
A1
|
CIT
|
C6 H8 O7
| 192.124
|
CITRIC ACID
|
InChI=1S/C6H8O7/c7-3(8)1-6(13,5(11)12)2-4(9)10/h13H,1-2H2,(H,7,8)(H,9,10)(H,11,12)
|
C(C(=O)O)C(CC(=O)O)(C(=O)O)O
| null | 8,108
|
7LFO
|
X-RAY DIFFRACTION
| 3.04
| 59.59
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
140 g/L PEG8000, 100 mM HEPES, 200 mM magnesium acetate, pH 7.5
| 277.15
|
2021-01-18
|
2021-05-26
| 2,455
| 1
| 329
| 146
| null | 38.46
| 1
|
1.94
|
experimental
| 47.258
| 0.243
| 0.2004
|
Protein Tyrosine Phosphatase 1B
|
MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPCRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTCGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHNLEHHHHHH
|
Protein
| 329
|
polypeptide(L)
| 1
| 38.437
|
Tyrosine-protein phosphatase non-receptor type 1
|
3.1.3.48
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 329
| 1
| 1
| 1
|
Monomer
|
A1
|
MG
|
Mg
| 24.305
|
MAGNESIUM ION
|
InChI=1S/Mg/q+2
|
[Mg+2]
| null | 5,836
|
8A2D
|
X-RAY DIFFRACTION
| 1.8
| 31.79
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
20% PEG Smear High, 0.1M MES
| 293
|
2022-06-03
|
2022-10-19
| 2,770
| 1
| 326
| 387
| null | 38.27
| 1
|
1.11
|
experimental
| 15.73
| 0.1788
| 0.1632
|
EGFR kinase domain (L858R/V948R) in complex with 2-[4-(difluoromethyl)-6-[2-[4-[[4-(hydroxymethyl)-1-piperidyl]methyl]phenyl]ethynyl]-7-methyl-indazol-2-yl]-2-spiro[6,7-dihydropyrrolo[1,2-c]imidazole-5,1'-cyclopropane]-1-yl-N-thiazol-2-yl-acetamide
|
GSMNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGRAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMRKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
|
Protein
| 326
|
polypeptide(L)
| 1
| 37.327
|
Epidermal growth factor receptor
|
2.7.10.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 326
| 1
| 1
| 1
|
Monomer
|
A1
|
EDO
|
C2 H6 O2
| 62.068
|
1,2-ETHANEDIOL
|
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
|
C(CO)O
| null | 11,536
|
5MPK
|
X-RAY DIFFRACTION
| 2.09
| 41.15
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
0.1 M HEPES-Na, pH7.5, 0.2 M MgCl2, 25% P3350
| 277
|
2016-12-16
|
2018-01-17
| 2,022
| 2
| 238
| 127
| null | 29.32
| 1
|
1.9
|
experimental
| null | 0.2391
| 0.1828
|
Crystal structure of CREBBP bromodomain complexed with DK19
|
SMRKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKNPMDLSTIKRKLDTGQYQEPWQYVDDVWLMFNNAWLYNRKTSRVYKFCSKLAEVFEQEIDPVMQSLG
|
Protein
| 119
|
polypeptide(L)
| 2
| 14.223
|
CREB-binding protein
|
2.3.1.48
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 119
| 1
| 1
| 1
|
Monomer
|
A1
|
0BC
|
C21 H18 N6 O3 S
| 434.471
|
~{N}-(5-ethanoyl-2-ethoxy-phenyl)-3-(2~{H}-1,2,3,4-tetrazol-5-yl)-5-(1,3-thiazol-4-yl)benzamide
|
InChI=1S/C21H18N6O3S/c1-3-30-19-5-4-13(12(2)28)9-17(19)23-21(29)16-7-14(18-10-31-11-22-18)6-15(8-16)20-24-26-27-25-20/h4-11H,3H2,1-2H3,(H,23,29)(H,24,25,26,27)
|
CCOc1ccc(cc1NC(=O)c2cc(cc(c2)c3n[nH]nn3)c4cscn4)C(=O)C
| null | 10,605
|
7PNR
|
X-RAY DIFFRACTION
| 2.29
| 46.21
|
VAPOR DIFFUSION, SITTING DROP
| null |
Malic acid/NaOH pH 7.0, PEG 3350
| 289
|
2021-09-07
|
2021-09-29
| 1,020
| 1
| 121
| 59
| 3
| 13.85
| 1
|
1.6
|
experimental
| 27.906
| 0.20103
| 0.18981
|
Human Angiogenin mutant-S28AT36AS37A
|
QDNSRYTHFLTQHYDAKPQGRDDRYCEAIMRRRGLAAPCKDINTFIHGNKRSIKAICENKNGNPHRENLRISKSSFQVTTCKLHGGSPWPPCQYRATAGFRNVVVACENGLPVHLDQSIFR
|
Protein
| 121
|
polypeptide(L)
| 1
| 13.853
|
Angiogenin
|
3.1.27
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 121
| 1
| 1
| 1
|
Monomer
|
A1
| null | null | null | null | null | null | null | 7,401
|
7U99
|
X-RAY DIFFRACTION
| 3.41
| 63.95
|
VAPOR DIFFUSION, HANGING DROP
| 6.5
|
0.1 M MES pH 6.5, 1.1 M Sodium Citrate
| 293
|
2022-03-10
|
2022-11-23
| 2,490
| 1
| 331
| 24
| null | 38.26
| 1
|
2.5
|
experimental
| 69.706
| 0.2139
| 0.187
|
EGFR kinase in complex with a macrocyclic inhibitor
|
GSTSGEAPNQALLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQQG
|
Protein
| 331
|
polypeptide(L)
| 1
| 37.636
|
Epidermal growth factor receptor
|
2.7.10.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 331
| 1
| 1
| 1
|
Monomer
|
A1
|
M0R
|
C21 H22 Cl N3 O5
| 431.869
|
19-chloro-22-methoxy-8,9,11,12,14,15-hexahydro-21H-4,6-ethenopyrimido[5,4-m][1,4,7,10,15]benzotetraoxazacycloheptadecine
|
InChI=1S/C21H22ClN3O5/c1-26-19-12-16-15-11-20(19)30-9-7-28-5-4-27-6-8-29-18-3-2-14(22)10-17(18)25-21(15)24-13-23-16/h2-3,10-13H,4-9H2,1H3,(H,23,24,25)
|
COc1cc2c3cc1OCCOCCOCCOc4ccc(cc4Nc3ncn2)Cl
|
Y
| 11,247
|
5QD3
|
X-RAY DIFFRACTION
| 3.16
| 61.08
|
hanging drop
| null |
CRYSTALS WERE GROWN AT 19C BY VAPOUR DIFFUSION IN HANGING DROPS FROM 1.0M AMMONIUM SULFATE IN WATER. PROTEIN STOCK WAS
BACE MUT46B BATCH XVI 7.0MG/ML IN 10MM TRIS-HCL PH 7.4, 25MM NACL, WITH A 6-FOLD EXCESS OF BMC010 ADDED FROM A 50MM
STOCK SOLUTION IN 90% DMSO-D6 (1.7% DMSO IN DROP). A SOLUTION CONTAINING 1.2M AMMONIUM SULFATE, 25% GLYCEROL, 1MM BMC010
AND 1.8% DMSO WAS USED AS CRYO-PROTECTANT.
| 292
|
2017-12-01
|
2020-06-03
| 9,374
| 3
| 1,206
| 353
| 9
| 135.9
| 1
|
2.46
|
experimental
| 47.78
| 0.2
| 0.164
|
Crystal structure of BACE complex with BMC010
|
GPDEEPEEPGRRGSFVEMVDNLRGKSGQGYYVEMTVGSPPQTLNILVDTGSSNFAVGAAPHPFLHRYYQRQLSSTYRDLRKGVYVPYTQGKWEGELGTDLVSIPHGPNVTVRANIAAITESDKFFINGSNWEGILGLAYAEIARPDDSLEPFFDSLVKQTHVPNLFSLQLCGAGFPLNQSEVLASVGGSMIIGGIDHSLYTGSLWYTPIRREWYYEVIIVRVEINGQDLKMDCKEYNYDKSIVDSGTTNLRLPKKVFEAAVKSIKAASSTEKFPDGFWLGEQLVCWQAGTTPWNIFPVISLYLMGEVTNQSFRITILPQQYLRPVEDVATSQDDCYKFAISQSSTGTVMGAVIMEGFYVVFDRARKRIGFAVSACHVHDEFRTAAVEGPFVTLDMEDCGYNI
|
Protein
| 402
|
polypeptide(L)
| 3
| 44.777
|
Beta-secretase 1
|
3.4.23.46
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 402
| 1
| 1
| 1
|
Monomer
|
A1
|
E6M
|
C32 H49 N3 O3
| 523.75
|
(10R,12S)-12-[(1R)-1-hydroxy-2-({[3-(propan-2-yl)phenyl]methyl}amino)ethyl]-17-(methoxymethyl)-10-methyl-2,13-diazabicyclo[13.3.1]nonadeca-1(19),15,17-trien-14-one
|
InChI=1S/C32H49N3O3/c1-23(2)27-13-10-12-25(16-27)20-33-21-31(36)30-15-24(3)11-8-6-5-7-9-14-34-29-18-26(22-38-4)17-28(19-29)32(37)35-30/h10,12-13,16-19,23-24,30-31,33-34,36H,5-9,11,14-15,20-22H2,1-4H3,(H,35,37)/t24-,30+,31-/m1/s1
|
CC1CCCCCCCNc2cc(cc(c2)C(=O)NC(C1)C(CNCc3cccc(c3)C(C)C)O)COC
| null | 2,907
|
8B78
|
X-RAY DIFFRACTION
| 2.75
| 55.23
|
VAPOR DIFFUSION, SITTING DROP
| null |
PEG 3350
LITHIUM SULFATE
| 293
|
2022-09-29
|
2023-07-12
| 1,524
| 1
| 168
| 124
| null | 20.11
| 1
|
1.11
|
experimental
| 20.835
| 0.2357
| 0.2236
|
KRasG12C ligand complex
|
GMTEYKLVVVGACGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETSLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKSDLPSRTVDTKQAQDLARSYGIPFIETSAKTRQRVDDAFYTLVREIRKHK
|
Protein
| 168
|
polypeptide(L)
| 1
| 19.195
|
GTPase KRas
|
3.6.5.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 168
| 1
| 1
| 1
|
Monomer
|
A1
|
MG
|
Mg
| 24.305
|
MAGNESIUM ION
|
InChI=1S/Mg/q+2
|
[Mg+2]
| null | 8,522
|
8B6M
|
X-RAY DIFFRACTION
| 2.65
| 53.5
|
VAPOR DIFFUSION, SITTING DROP
| 8.5
|
100 mM Tris, 22% w/v PEG3350, 200 mM Li2SO4, 250 mM NaCl, 20% v/v glycerol
| 277.15
|
2022-09-27
|
2023-10-11
| 3,703
| 4
| 438
| 200
| null | 51.41
| 2
|
1.6
|
experimental
| 27.2
| 0.2194
| 0.1849
|
Tankyrase 2 in complex with an inhibitor
|
SMLNTSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGIFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPVHKDRSCYICHRQLLFCRVTLGKSFLQFSAMK
|
Protein
| 171
|
polypeptide(L)
| 2
| 19.482
|
Poly [ADP-ribose] polymerase tankyrase-2
|
2.4.2.30
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 219
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
OY6
|
C30 H27 N5 O4 S
| 553.631
|
~{N}-(2-methoxyphenyl)-4-[[2-(4-oxidanylidene-3~{H}-quinazolin-2-yl)ethyl-(thiophen-2-ylmethyl)carbamoyl]amino]benzamide
|
InChI=1S/C30H27N5O4S/c1-39-26-11-5-4-10-25(26)33-28(36)20-12-14-21(15-13-20)31-30(38)35(19-22-7-6-18-40-22)17-16-27-32-24-9-3-2-8-23(24)29(37)34-27/h2-15,18H,16-17,19H2,1H3,(H,31,38)(H,33,36)(H,32,34,37)
|
COc1ccccc1NC(=O)c2ccc(cc2)NC(=O)N(CCC3=Nc4ccccc4C(=O)N3)Cc5cccs5
|
Y
| 6,429
|
5NIA
|
X-RAY DIFFRACTION
| 2.46
| 50
|
VAPOR DIFFUSION, HANGING DROP
| null |
8% (w/v) PEG 20 000, 15% (w/v) PEG MME 550, 100 mM Hepes/MOPS pH 7.7-8.0, 15 mM CaCl2, 15 mM MgCl2
| 294
|
2017-03-23
|
2017-08-23
| 5,308
| 1
| 617
| 360
| null | 70.26
| 1
|
1.764
|
experimental
| 47.94
| 0.2074
| 0.1801
|
Crystal structure of human LTA4H mutant D375N in open conformation (crystal form I)
|
MHHHHHHPEIVDTCSLASPASVCRTKHLHLRCSVDFTRRTLTGTAALTVQSQEDNLRSLVLDTKDLTIEKVVINGQEVKYALGERQSYKGSPMEISLPIALSKNQEIVIEISFETSPKSSALQWLTPEQTSGKEHPYLFSQCQAIHCRAILPCQDTPSVKLTYTAEVSVPKELVALMSAIRDGETPDPEDPSRKIYKFIQKVPIPCYLIALVVGALESRQIGPRTLVWSEKEQVEKSAYEFSETESMLKIAEDLGGPYVWGQYDLLVLPPSFPYGGMENPCLTFVTPTLLAGDKSLSNVIAHEISHSWTGNLVTNKTWDHFWLNEGHTVYLERHICGRLFGEKFRHFNALGGWGELQNSVKTFGETHPFTKLVVDLTDIDPNVAYSSVPYEKGFALLFYLEQLLGGPEIFLGFLKAYVEKFSYKSITTDDWKDFLYSYFKDKVDVLNQVDWNAWLYSPGLPPIKPNYDMTLTNACIALSQRWITAKEDDLNSFNATDLKDLSSHQLNEFLAQTLQRAPLPLGHIKRMQEVYNFNAINNSEIRFRWLRLCIQSKWEDAIPLALKMATEQGRMKFTRPLFKDLAAFDKSHDQAVRTYQEHKASMHPVTAMLVGKDLKVD
|
Protein
| 617
|
polypeptide(L)
| 1
| 70.192
|
Leukotriene A-4 hydrolase
|
3.3.2.6
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 617
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 3,538
|
7A2H
|
X-RAY DIFFRACTION
| 2.67
| 53.88
|
VAPOR DIFFUSION, SITTING DROP
| null |
Reservoir composition: 28 % (w/v) PEG6000, 0.9 M LiCl, 0.1 M, Tris/HCl, pH 8.5; drop composition prior to equilibration: 0.01 ml reservoir solution + 0.02 ml CK2alpha' (mutant Cys336Ser)/inhibitor MB002 mixture (0.180 ml 6 mg/ml CK2alpha'Cys336Ser, 0.5 M NaCl, 25 mM Tris/HCl, pH 8.5, mixed and pre-equilibrated with 0.02 ml 10 mM MB002 in dimethyl sulfoxide); the initial inhibitor MB002 was replaced by the inhibitor 5,6,7-tribromo-1H-imidazo[4,5-b]pyridine by extensive crystal soaking.
| 293
|
2020-08-18
|
2020-12-09
| 3,304
| 1
| 364
| 433
| null | 43.42
| 1
|
1.01
|
experimental
| 17.38
| 0.1495
| 0.1426
|
Crystal structure of human protein kinase CK2alpha' (CSNK2A2 gene product) in complex with the ATP-competitive inhibitor 5,6,7-tribromo-1H-imidazo[4,5-b]pyridine
|
MGSSHHHHHHSQDPMPGPAAGSRARVYAEVNSLRSREYWDYEAHVPSWGNQDDYQLVRKLGRGKYSEVFEAINITNNERVVVKILKPVKKKKIKREVKILENLRGGTNIIKLIDTVKDPVSKTPALVFEYINNTDFKQLYQILTDFDIRFYMYELLKALDYCHSKGIMHRDVKPHNVMIDHQQKKLRLIDWGLAEFYHPAQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRREPFFHGQDNYDQLVRIAKVLGTEELYGYLKKYHIDLDPHFNDILGQHSRKRWENFIHSENRHLVSPEALDLLDKLLRYDHQQRLTAKEAMEHPYFYPVVKEQSQPSADNAVLSSGLTAAR
|
Protein
| 364
|
polypeptide(L)
| 1
| 42.88
|
Casein kinase II subunit alpha'
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 364
| 1
| 1
| 1
|
Monomer
|
A1
|
QX2
|
C6 H2 Br3 N3
| 355.812
|
5,6,7-tris(bromanyl)-1~{H}-imidazo[4,5-b]pyridine
|
InChI=1S/C6H2Br3N3/c7-2-3(8)5(9)12-6-4(2)10-1-11-6/h1H,(H,10,11,12)
|
c1[nH]c2c(c(c(nc2n1)Br)Br)Br
|
Y
| 2,133
|
6T7Q
|
X-RAY DIFFRACTION
| 2.18
| 43.67
|
VAPOR DIFFUSION, HANGING DROP
| 5
|
50 mM Di-Ammoniumhydrogen citrate pH 5.0: 15 mg/mL hAR, 5.2 mg/mL DTT, 0.7 mg/mL NADP+, 5% (w/v) PEG 6000
Reservoir: 120 mM Di-Ammoniumhydrogen citrate pH 5.0, 20% (w/v) PEG 6000
Soaking-buffer: 120 mM Di-Ammoniumhydrogen citrate pH 5.0, 25% (w/v) PEG 6000
| 291
|
2019-10-23
|
2020-11-18
| 3,233
| 1
| 316
| 409
| null | 37.14
| 1
|
1.01
|
experimental
| 11.81
| 0.1322
| 0.1177
|
Human Aldose Reductase Mutant L301A in Complex with a Ligand with an IDD Structure (3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic acid)
|
MASRILLNNGAKMPILGLGTWKSPPGQVTEAVKVAIDVGYRHIDCAHVYQNENEVGVAIQEKLREQVVKREELFIVSKLWCTYHEKGLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKEFFPLDESGNVVPSDTNILDTWAAMEELVDEGLVKAIGISNFNHLQVEMILNKPGLKYKPAVNQIECHPYLTQEKLIQYCQSKGIVVTAYSPLGSPDRPWAKPEDPSLLEDPRIKAIAAKHNKTTAQVLIRFPMQRNLVVIPKSVTPERIAENFKVFDFELSSQDMTTLLSYNRNWRVCALASCTSHKDYPFHEEF
|
Protein
| 316
|
polypeptide(L)
| 1
| 35.856
|
Aldo-keto reductase family 1 member B1
|
1.1.1.300
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 316
| 1
| 1
| 1
|
Monomer
|
A1
|
4G7
|
C17 H14 F N O6
| 347.295
|
3-({[2-(carboxymethoxy)-4-fluorobenzoyl]amino}methyl)benzoic acid
|
InChI=1S/C17H14FNO6/c18-12-4-5-13(14(7-12)25-9-15(20)21)16(22)19-8-10-2-1-3-11(6-10)17(23)24/h1-7H,8-9H2,(H,19,22)(H,20,21)(H,23,24)
|
c1cc(cc(c1)C(=O)O)CNC(=O)c2ccc(cc2OCC(=O)O)F
|
Y
| 1,897
|
5RW3
|
X-RAY DIFFRACTION
| 2.11
| 41.62
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulfate, 100 mM MES/imidazole, pH 6.5, 20% PEG500 MME, 10% PEG20000
| 293
|
2020-10-30
|
2020-11-11
| 4,745
| 1
| 463
| 442
| null | 53.35
| 1
|
1.37
|
experimental
| 18.421
| 0.196
| 0.1707
|
INPP5D PanDDA analysis group deposition -- Crystal Structure of the phosphatase and C2 domains of SHIP1 in complex with Z2064898339
|
SMEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQ
|
Protein
| 463
|
polypeptide(L)
| 1
| 52.878
|
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
|
3.1.3.86
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 463
| 1
| 1
| 1
|
Monomer
|
A1
|
WLY
|
C14 H19 N O2
| 233.306
|
2-(4-methylphenyl)-N-{[(2S)-oxolan-2-yl]methyl}acetamide
|
InChI=1S/C14H19NO2/c1-11-4-6-12(7-5-11)9-14(16)15-10-13-3-2-8-17-13/h4-7,13H,2-3,8-10H2,1H3,(H,15,16)/t13-/m0/s1
|
Cc1ccc(cc1)CC(=O)NCC2CCCO2
| null | 8,188
|
8FPW
|
X-RAY DIFFRACTION
| 2.31
| 46.85
|
VAPOR DIFFUSION, HANGING DROP
| 8
|
20-24% PEG8K, 15% Dioxane, 0.1M Tris pH8.0
| 277
|
2023-01-05
|
2024-06-05
| 1,756
| 1
| 183
| 231
| null | 21.25
| 1
|
1.4
|
experimental
| null | 0.2079
| 0.1781
|
Crystal structure of tumor related RhoA mutant A161V in complex with GDP
|
GSMAAIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSVKTKDGVREVFEMATRAALQA
|
Protein
| 183
|
polypeptide(L)
| 1
| 20.607
|
Transforming protein RhoA
|
3.6.5.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 183
| 1
| 1
| 1
|
Monomer
|
A1
|
MG
|
Mg
| 24.305
|
MAGNESIUM ION
|
InChI=1S/Mg/q+2
|
[Mg+2]
|
Y
| 11,438
|
6FCK
|
X-RAY DIFFRACTION
| 2.42
| 49.1
|
VAPOR DIFFUSION, HANGING DROP
| null |
16% Peg8k, 0.1M Caco pH 6.8, 0.15M AS
| 298
|
2017-12-20
|
2018-01-17
| 2,554
| 1
| 276
| 331
| null | 32.27
| 1
|
1.9
|
experimental
| 21.7
| 0.214
| 0.174
|
CHK1 KINASE IN COMPLEX WITH COMPOUND 13
|
MAVPFVEDWDLVQTLGEGAYGEVQLAVNRVTEEAVAVKIVDMKRAVDCPENIKKEICINKMLNHENVVKFYGHRREGNIQYLFLEYCSGGELFDRIEPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRP
|
Protein
| 276
|
polypeptide(L)
| 1
| 31.841
|
Serine/threonine-protein kinase Chk1
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 276
| 1
| 1
| 1
|
Monomer
|
A1
|
D4Z
|
C20 H22 N4 O
| 334.415
|
2-phenyl-4-[[(3~{S})-piperidin-3-yl]amino]-1~{H}-indole-7-carboxamide
|
InChI=1S/C20H22N4O/c21-20(25)15-8-9-17(23-14-7-4-10-22-12-14)16-11-18(24-19(15)16)13-5-2-1-3-6-13/h1-3,5-6,8-9,11,14,22-24H,4,7,10,12H2,(H2,21,25)/t14-/m0/s1
|
c1ccc(cc1)c2cc3c(ccc(c3[nH]2)C(=O)N)NC4CCCNC4
|
Y
| 8,713
|
5OYF
|
X-RAY DIFFRACTION
| 1.98
| 37.81
|
VAPOR DIFFUSION, HANGING DROP
| 6.5
|
112.5mM Mes pH 6.5, 35% glycerol ethoxylate, 180 mM ammonium acetate
| 298
|
2017-09-08
|
2018-02-28
| 3,086
| 1
| 342
| 201
| null | 41.64
| 1
|
1.54
|
experimental
| 30.35
| 0.216
| 0.185
|
The crystal structure of CK2alpha in complex with compound 31
|
SGPVPSRARVYTDVNTHRPSEYWDYESHVVEWGNQDDYQLVRKLGRGKYSEVFEAINITNNEKVVVKILKPVAAAKIKREIKILENLRGGPNIITLADIVKDPVSRTPALVFEHVNNTDFKQLYQTLTDYDIRFYMYEILKALDYCHSMGIMHRDVKPHNVMIDHEHRKLRLIDWGLAEFYHPGQEYNVRVASRYFKGPELLVDYQMYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTEDLYDYIDKYNIELDPRFNDILGRHSRKRWERFVHSENQHLVSPEALDFLDKLLRYDHQSRLTAREAMEHPYFYTVVKREAMEHPYFYTVVK
|
Protein
| 342
|
polypeptide(L)
| 1
| 40.786
|
Casein kinase II subunit alpha
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 342
| 1
| 1
| 1
|
Monomer
|
A1
|
B4Q
|
C25 H27 N3
| 369.502
|
2-(1~{H}-benzimidazol-2-yl)-~{N}-[[4-(2-ethylphenyl)-3-methyl-phenyl]methyl]ethanamine
|
InChI=1S/C25H27N3/c1-3-20-8-4-5-9-22(20)21-13-12-19(16-18(21)2)17-26-15-14-25-27-23-10-6-7-11-24(23)28-25/h4-13,16,26H,3,14-15,17H2,1-2H3,(H,27,28)
|
CCc1ccccc1c2ccc(cc2C)CNCCc3[nH]c4ccccc4n3
|
Y
| 5,180
|
6YVY
|
X-RAY DIFFRACTION
| 2.82
| 56.34
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
15% PEG 3350
| 294
|
2020-04-28
|
2021-02-10
| 9,023
| 4
| 1,128
| 507
| 4
| 131.15
| 1
|
1.918
|
experimental
| 39.24
| 0.2353
| 0.2141
|
FOCAL ADHESION KINASE CATALYTIC DOMAIN IN COMPLEX WITH 4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide
|
GSGSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEE
|
Protein
| 282
|
polypeptide(L)
| 4
| 32.304
|
Focal adhesion kinase 1
|
2.7.10.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 282
| 1
| 1
| 1
|
Monomer
|
A1
|
P1E
|
C19 H25 F3 N6 O2 S
| 458.501
|
4-{[4-{[(1R,2R)-2-(dimethylamino)cyclopentyl]amino}-5-(trifluoromethyl)pyrimidin-2-yl]amino}-N-methylbenzenesulfonamide
|
InChI=1S/C19H25F3N6O2S/c1-23-31(29,30)13-9-7-12(8-10-13)25-18-24-11-14(19(20,21)22)17(27-18)26-15-5-4-6-16(15)28(2)3/h7-11,15-16,23H,4-6H2,1-3H3,(H2,24,25,26,27)/t15-,16-/m1/s1
|
CNS(=O)(=O)c1ccc(cc1)Nc2ncc(c(n2)NC3CCCC3N(C)C)C(F)(F)F
|
Y
| 9,174
|
5VUB
|
X-RAY DIFFRACTION
| 3.27
| 62.43
|
VAPOR DIFFUSION, HANGING DROP
| 5.5
|
100MM CITRATE BUFFER, PH 5.5, 200MM NACL, 1M NH4HPO4
| 293
|
2017-05-18
|
2017-12-13
| 2,501
| 1
| 298
| 238
| null | 34.69
| 1
|
2.0
|
experimental
| 32.39
| 0.1837
| 0.1603
|
Pim1 Kinase in complex with a benzofuranone inhibitor
|
MKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSKSGPSSGENLYFQ
|
Protein
| 298
|
polypeptide(L)
| 1
| 34.204
|
Serine/threonine-protein kinase pim-1
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 298
| 1
| 1
| 1
|
Monomer
|
A1
|
GOL
|
C3 H8 O3
| 92.094
|
GLYCEROL
|
InChI=1S/C3H8O3/c4-1-3(6)2-5/h3-6H,1-2H2
|
C(C(CO)O)O
| null | 8,067
|
5NK9
|
X-RAY DIFFRACTION
| 1.96
| 37.36
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
37.5% MPD/PEG1000/PEG3350 (MD), 0.1 M Amino Acids Mix (MD), 0.1 M Hepes pH6.5
| 291
|
2017-03-31
|
2017-06-07
| 2,653
| 1
| 306
| 261
| null | 34.96
| 1
|
1.588
|
experimental
| null | 0.1945
| 0.1621
|
Crystal Structure of Ephrin A2 (EphA2) Receptor Protein Kinase with Compound 2e
|
GDPNQAVLKFTTEIHPSCVTRQKVIGAGEFGEVYKGMLKTSSGKKEVPVAIKTLKAGYTEKQRVDFLGEAGIMGQFSHHNIIRLEGVISKYKPMMIITEYMENGALDKFLREKDGEFSVLQLVGMLRGIAAGMKYLANMNYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEATYTTSGGKIPIRWTAPEAISYRKFTSASDVWSFGIVMWEVMTYGERPYWELSNHEVMKAINDGFRLPTPMDCPSAIYQLMMQCWQQERARRPKFADIVSILDKLIRAPDSLKTLADFDPRVSIRLPSTSG
|
Protein
| 306
|
polypeptide(L)
| 1
| 34.463
|
Ephrin type-A receptor 2
|
2.7.10.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 306
| 1
| 1
| 1
|
Monomer
|
A1
|
912
|
C25 H29 Cl N4 O3 S
| 501.041
|
(2~{Z})-~{N}-(2-chloranyl-6-methyl-phenyl)-2-[3-[(4-methyl-4-oxidanyl-cyclohexyl)carbamoyl]phenyl]imino-1,3-thiazolidine-5-carboxamide
|
InChI=1S/C25H29ClN4O3S/c1-15-5-3-8-19(26)21(15)30-23(32)20-14-27-24(34-20)29-18-7-4-6-16(13-18)22(31)28-17-9-11-25(2,33)12-10-17/h3-8,13,17,20,33H,9-12,14H2,1-2H3,(H,27,29)(H,28,31)(H,30,32)/t17-,20-,25-/m1/s1
|
Cc1cccc(c1NC(=O)C2CNC(=Nc3cccc(c3)C(=O)NC4CCC(CC4)(C)O)S2)Cl
| null | 7,746
|
5EHV
|
X-RAY DIFFRACTION
| 2.08
| 40.81
|
VAPOR DIFFUSION, SITTING DROP
| null |
ammonium sulfate, tris-chloride
| 280
|
2015-10-29
|
2016-03-09
| 2,578
| 1
| 260
| 382
| null | 29.83
| 1
|
1.208
|
experimental
| null | 0.1746
| 0.1532
|
human carbonic anhydrase II in complex with ligand
|
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Protein
| 260
|
polypeptide(L)
| 1
| 29.289
|
Carbonic anhydrase 2
|
4.2.1.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 260
| 1
| 1
| 1
|
Monomer
|
A1
|
5ON
|
C18 H16 O5
| 312.317
|
(~{E})-3-[3-[[3-(2-hydroxy-2-oxoethyl)phenyl]methoxy]phenyl]prop-2-enoic acid
|
InChI=1S/C18H16O5/c19-17(20)8-7-13-3-2-6-16(10-13)23-12-15-5-1-4-14(9-15)11-18(21)22/h1-10H,11-12H2,(H,19,20)(H,21,22)/b8-7+
|
c1cc(cc(c1)COc2cccc(c2)C=CC(=O)O)CC(=O)O
| null | 1,817
|
5VLR
|
X-RAY DIFFRACTION
| 2.6
| 53.2
|
VAPOR DIFFUSION
| null |
NULL, VAPOR DIFFUSION, TEMPERATURE
293K
| 300
|
2017-04-26
|
2017-06-07
| 8,448
| 2
| 1,183
| 24
| null | 137.48
| 2
|
2.8
|
experimental
| 87.32
| 0.279
| 0.208
|
CRYSTAL STRUCTURE OF PI3K DELTA IN COMPLEX WITH A TRIFLUORO-ETHYL-PYRAZOL-PYROLOTRIAZINE INHIBITOR
|
NQSVVVDFLLPTGVYLNFPVSRNANLSTIKQLLWHRAQYEPLFHMLSGPEAYVFTCINQTAEQQELEDEQRRLCDVQPFLPVLRLVAREGDRVKKLINSQISLLIGKGLHEFDSLCDPEVNDFRAKMCQFCEEAAARRQQLGWEAWLQYSFPLQLEPSAQTWGPGTLRLPNRALLVNVKFEGSEESFTFQVSTKDVPLALMACALRKKATVFRQPLVEQPEDYTLQVNGRHEYLYGSYPLCQFQYICSCLHSGLTPHLTMVHSSSILAMRDEQSNPAPQVQKPRAKPPPIPAKKPSSVSLWSLEQPFRIELIQGSKVNADERMKLVVQAGLFHGNEMLCKTVSSSEVSVCSEPVWKQRLEFDINICDLPRMARLCFALYAVIEKAKKARSTKKKSKKADCPIAWANLMLFDYKDQLKTGERCLYMWPSVPDEKGELLNPTGTVRSNPNTDSAAALLICLPEVAPHPVYYPALEKILELGRHSECVHVTEEEQLQLREILERRGSGELYEHEKDLVWKLRHEVQEHFPEALARLLLVTKWNKHEDVAQMLYLLCSWPELPVLSALELLDFSFPDCHVGSFAIKSLRKLTDDELFQYLLQLVQVLKYESYLDCELTKFLLDRALANRKIGHFLFWHLRSEMHVPSVALRFGLILEAYCRGSTHHMKVLMKQGEALSKLKALNDFVKLSSQKTPKPQTKELMHLCMRQEAYLEALSHLQSPLDPSTLLAEVCVEQCTFMDSKMKPLWIMYSNEEAGSGGSVGIIFKNGDDLRQDMLTLQMIQLMDVLWKQEGLDLRMTPYGCLPTGDRTGLIEVVLRSDTIANIQLNKSNMAATAAFNKDALLNWLKSKNPGEALDRAIEEFTLSCAGYCVATYVLGIGDRHSDNIMIRESGQLFHIDFGHFLGNFKTKFGINRERVPFILTYDFVHVIQQGKTNNSEKFERFRGYCERAYTILRRHGLLFLHLFALMRAAGLPELSCSKDIQYLKDSLALGKTEEEALKHFRVKFNEALRESWKT
|
Protein
| 1,013
|
polypeptide(L)
| 1
| 115.959
|
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
|
2.7.1.153
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 1,013
| 1
| 1
| 1
|
Monomer
|
A1
|
9EM
|
C25 H25 F3 N8 O2
| 526.514
|
4-acetyl-1-(3-{4-amino-5-[1-(2,2,2-trifluoroethyl)-1H-pyrazol-5-yl]pyrrolo[2,1-f][1,2,4]triazin-7-yl}phenyl)-3,3-dimethylpiperazin-2-one
|
InChI=1S/C25H25F3N8O2/c1-15(37)34-10-9-33(23(38)24(34,2)3)17-6-4-5-16(11-17)20-12-18(21-22(29)30-14-32-36(20)21)19-7-8-31-35(19)13-25(26,27)28/h4-8,11-12,14H,9-10,13H2,1-3H3,(H2,29,30,32)
|
CC(=O)N1CCN(C(=O)C1(C)C)c2cccc(c2)c3cc(c4n3ncnc4N)c5ccnn5CC(F)(F)F
| null | 11,551
|
5R56
|
X-RAY DIFFRACTION
| 2.01
| 38.94
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
0.1M HEPES pH 7.5, 0.3M sodium/potassium phosphate, 15% PEG Smear High, 20% ethylene glycol
| 277
|
2020-02-28
|
2020-07-01
| 2,458
| 1
| 304
| 163
| null | 33.43
| 1
|
1.51
|
experimental
| 24.013
| 0.2156
| 0.1839
|
PanDDA analysis group deposition -- Crystal Structure of human NUDT22 in complex with N13688a
|
SMDPEVTLLLQCPGGGLPQEQIQAELSPAHDRRPLPGGDEAITAIWETRLKAQPWLFDAPKFRLHSATLAPIGSRGPQLLLRLGLTSYRDFLGTNWSSSAAWLRQQGATDWGDTQAYLADPLGVGAALATADDFLVFLRRSRQVAEAPGLVDVPGGHPEPQALCPGGSPQHQDLAGQLVVHELFSSVLQEICDEVNLPLLTLSQPLLLGIARNETSAGRASAEFYVQCSLTSEQVRKHYLSGGPEAHESTGIFFVETQNVRRLPETEMWAELCPSAKGAIILYNRVQGSPTGAALGSPALLPPL
|
Protein
| 304
|
polypeptide(L)
| 1
| 32.707
|
Uridine diphosphate glucose pyrophosphatase NUDT22
|
3.6.1.45
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 304
| 1
| 1
| 1
|
Monomer
|
A1
|
S07
|
C14 H19 N O3
| 249.306
|
2-(2,4-dimethylphenoxy)-1-morpholin-4-yl-ethanone
|
InChI=1S/C14H19NO3/c1-11-3-4-13(12(2)9-11)18-10-14(16)15-5-7-17-8-6-15/h3-4,9H,5-8,10H2,1-2H3
|
Cc1ccc(c(c1)C)OCC(=O)N2CCOCC2
| null | 1,937
|
4YXO
|
X-RAY DIFFRACTION
| 2.08
| 40.75
|
VAPOR DIFFUSION, HANGING DROP
| 7.8
|
2.5 uL of the protein solution (10 mg/ml hCAII in 50 mM Tris pH 7.8) were mixed with 2.5 uL of the well solution (2.7 M (NH4)SO4, 100 mM Tris, pH 7.8, saturated with p-chloromercurybenzoicacid) and placed as a hanging drop. Crystals appeared after several days. The crystals were soaked in 3.0 M (NH4)SO4, 100 mM Tris, pH 7.8, saturated with the inhibitor, for 1 day.
| 291
|
2015-03-23
|
2016-02-03
| 2,362
| 1
| 260
| 239
| null | 30.14
| 1
|
1.06
|
experimental
| null | 0.164
| 0.1486
|
Human Carbonic Anhydrase II complexed with an inhibitor with a benzenesulfonamide group (3).
|
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Protein
| 260
|
polypeptide(L)
| 1
| 29.289
|
Carbonic anhydrase 2
|
4.2.1.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 260
| 1
| 1
| 1
|
Monomer
|
A1
|
MBO
|
C7 H5 Hg O2
| 321.703
|
MERCURIBENZOIC ACID
|
InChI=1S/C7H5O2.Hg/c8-7(9)6-4-2-1-3-5-6;/h2-5H,(H,8,9);
|
c1cc(ccc1C(=O)O)[Hg]
| null | 337
|
7U4I
|
X-RAY DIFFRACTION
| 2.18
| 43.47
|
MICROBATCH
| 7
|
0.2 M potassium thiocyanate and 20% (w/v) PEG 3350
| 291
|
2022-02-28
|
2022-12-07
| 2,811
| 2
| 384
| 179
| null | 44.32
| 1
|
1.97
|
experimental
| 31.7419
| 0.2458
| 0.2007
|
Crystal structure of human GPX4-U46C-R152H in complex with CDS9
|
MGSSHHHHHHSSGLVPRGSHMLEAASRDDWRCARSMHEFSAKDIDGHMVNLDKYRGFVCIVTNVASQCGKTEVNYTQLVDLHARYAECGLRILAFPCNQFGKQEPGSNEEIKEFAAGYNVKFDMFSKICVNGDDAHPLWKWMKIQPKGKGILGNAIKWNFTKFLIDKNGCVVKHYGPMEEPLVIEKDLPHYF
|
Protein
| 192
|
polypeptide(L)
| 2
| 21.869
|
Phospholipid hydroperoxide glutathione peroxidase
|
1.11.1.12
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 192
| 1
| 1
| 1
|
Monomer
|
A1
|
L9U
|
C7 H8 Br N O S
| 234.114
|
2-bromo-N-[(thiophen-2-yl)methyl]acetamide
|
InChI=1S/C7H8BrNOS/c8-4-7(10)9-5-6-2-1-3-11-6/h1-3H,4-5H2,(H,9,10)
|
c1cc(sc1)CNC(=O)CBr
| null | 2,335
|
5KW2
|
X-RAY DIFFRACTION
| 3.12
| 60.54
|
LIPIDIC CUBIC PHASE
| null |
0.1 M Tris HCl, pH 8.5, 30% PEG 400, 0.2 M ammonium formate.
| 298
|
2016-07-15
|
2018-05-02
| 3,237
| 1
| 491
| 52
| 1
| 53.73
| 1
|
2.76
|
experimental
| 41.374
| 0.2727
| 0.2304
|
The extra-helical binding site of GPR40 and the structural basis for allosteric agonism and incretin stimulation
|
MDYKDDDDKGSATMDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSAVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFAPLYAGGGFLAALSAARYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCFVGCLRALARGSNIFEMLRIDEGLRLKIYKDTEGYYTIGIGHLLTKSPSLNAAKSELDKAIGRNTNGVITKDEAEKLFNQDVDAAVRGILRNAKLKPVYDSLDAVRRAALINMVFQMGETGVAGFTNSLRMLQQKRWDEAAVNLAKSRWYNQTPNRAKRVITTFRTGTWDAYGSLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQKAENLYFQGHHHHHHHH
|
Protein
| 491
|
polypeptide(L)
| 1
| 53.102
|
Free fatty acid receptor 1,Lysozyme,Free fatty acid receptor 1
|
3.2.1.17
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 491
| 1
| 1
| 1
|
Monomer
|
A1
|
6XQ
|
C38 H45 N3 O5
| 623.781
|
(3~{S})-3-cyclopropyl-3-[2-[1-[2-[2,2-dimethylpropyl-(6-methylpyridin-2-yl)carbamoyl]-5-methoxy-phenyl]piperidin-4-yl]-1-benzofuran-6-yl]propanoic acid
|
InChI=1S/C38H45N3O5/c1-24-7-6-8-35(39-24)41(23-38(2,3)4)37(44)30-14-13-29(45-5)21-32(30)40-17-15-26(16-18-40)33-20-28-12-11-27(19-34(28)46-33)31(22-36(42)43)25-9-10-25/h6-8,11-14,19-21,25-26,31H,9-10,15-18,22-23H2,1-5H3,(H,42,43)/t31-/m0/s1
|
Cc1cccc(n1)N(CC(C)(C)C)C(=O)c2ccc(cc2N3CCC(CC3)c4cc5ccc(cc5o4)C(CC(=O)O)C6CC6)OC
| null | 4,395
|
5SKJ
|
X-RAY DIFFRACTION
| 2.6
| 52.74
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
5-20 mg/mL protein in 25mM HEPES/NaOH pH7.5, 150mM NaCl, 50mM BME mixed 1:1 with reservoir 0.1M HEPES/NaOH pH7.5, 30% PEG550MME, 50mM MgCl2
| 295
|
2022-02-01
|
2022-10-12
| 10,527
| 4
| 1,372
| 277
| 4
| 159.22
| 1
|
2.74
|
experimental
| 45.162
| 0.2489
| 0.166
|
Crystal Structure of human phosphodiesterase 10 in complex with 6-cyclopropyl-N-[2-[2-(methylamino)-2-oxoethyl]phenyl]-3-(pyrimidin-5-ylamino)pyridine-2-carboxamide
|
GSSICTSEEWQGLMQFTLPVRLCKEIELFHFDIGPFENMWPGIFVYMVHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNHTLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLNNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKKDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLSQWEKVIRGEETATWISSPSVAQKAAASED
|
Protein
| 343
|
polypeptide(L)
| 4
| 39.413
|
cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
|
3.1.4.17
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 343
| 1
| 1
| 1
|
Monomer
|
A1
|
KG3
|
C22 H22 N6 O2
| 402.449
|
6-cyclopropyl-N-{2-[2-(methylamino)-2-oxoethyl]phenyl}-3-[(pyrimidin-5-yl)amino]pyridine-2-carboxamide
|
InChI=1S/C22H22N6O2/c1-23-20(29)10-15-4-2-3-5-17(15)28-22(30)21-19(26-16-11-24-13-25-12-16)9-8-18(27-21)14-6-7-14/h2-5,8-9,11-14,26H,6-7,10H2,1H3,(H,23,29)(H,28,30)
|
CNC(=O)Cc1ccccc1NC(=O)c2c(ccc(n2)C3CC3)Nc4cncnc4
|
Y
| 2,072
|
8T2H
|
X-RAY DIFFRACTION
| 2.27
| 45.86
|
VAPOR DIFFUSION, HANGING DROP
| 6
|
1.8 M sodium malonate, 1.3% PEG 400
| 298
|
2023-06-06
|
2024-05-15
| 6,053
| 2
| 730
| 354
| null | 86.18
| 1
|
1.85
|
experimental
| 21.451
| 0.21303
| 0.16329
|
DYRK1A complex with DYR530
|
DSSHKKERKVYNDGYDDDNYDYIVKNGEKWMDRYEIDSLIGKGSFGQVVKAYDRVEQEWVAIKIIKNKKAFLNQAQIEVRLLELMNKHDTEMKYYIVHLKRHFMFRNHLCLVFEMLSYNLYDLLRNTNFRGVSLNLTRKFAQQMCTALLFLATPELSIIHCDLKPENILLCNPKRSAIKIVDFGSSCQLGQRIYQYIQSRFYRSPEVLLGMPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIVEVLGIPPAHILDQAPKARKFFEKLPDGTWNLKKTKDGKREYKPPGTRKLHNILGVETGGPGGRRAGESGHTVADYLKFKDLILRMLDYDPKTRIQPYYALQHSFFKKTADEGTNTS
|
Protein
| 365
|
polypeptide(L)
| 2
| 42.439
|
Dual specificity tyrosine-phosphorylation-regulated kinase 1A
|
2.7.11.23
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 365
| 1
| 1
| 1
|
Monomer
|
A1
|
XIR
|
C23 H24 F N7
| 417.482
|
(4P)-4-{(3M)-3-[3-fluoro-4-(4-methylpiperazin-1-yl)phenyl]-2-methyl-3H-imidazo[4,5-b]pyridin-5-yl}pyridin-2-amine
|
InChI=1S/C23H24FN7/c1-15-27-20-5-4-19(16-7-8-26-22(25)13-16)28-23(20)31(15)17-3-6-21(18(24)14-17)30-11-9-29(2)10-12-30/h3-8,13-14H,9-12H2,1-2H3,(H2,25,26)
|
Cc1nc2ccc(nc2n1c3ccc(c(c3)F)N4CCN(CC4)C)c5ccnc(c5)N
|
Y
| 8,639
|
7RNY
|
X-RAY DIFFRACTION
| 2.09
| 41.06
|
VAPOR DIFFUSION, HANGING DROP
| 7.8
|
1.6 M sodium citrate, 50 mM tris base
| 293
|
2021-07-30
|
2022-06-08
| 2,323
| 1
| 260
| 215
| null | 29.77
| 1
|
1.29
|
experimental
| 12.871
| 0.174
| 0.154
|
Carbonic Anhydrase II in complex with 3-ureido benzenesulfonamide derivative
|
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Protein
| 260
|
polypeptide(L)
| 1
| 29.289
|
Carbonic anhydrase 2
|
4.2.1.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 260
| 1
| 1
| 1
|
Monomer
|
A1
|
65M
|
C15 H17 N3 O3 S
| 319.379
|
3-{[benzyl(methyl)carbamoyl]amino}benzene-1-sulfonamide
|
InChI=1S/C15H17N3O3S/c1-18(11-12-6-3-2-4-7-12)15(19)17-13-8-5-9-14(10-13)22(16,20)21/h2-10H,11H2,1H3,(H,17,19)(H2,16,20,21)
|
CN(Cc1ccccc1)C(=O)Nc2cccc(c2)S(=O)(=O)N
|
Y
| 1,726
|
5CLS
|
X-RAY DIFFRACTION
| 2.74
| 55.08
|
VAPOR DIFFUSION, SITTING DROP
| 5.4
|
Na Citrate, Tert-butanol
| 292
|
2015-07-16
|
2016-01-13
| 3,351
| 1
| 371
| 329
| 1
| 42.51
| 1
|
1.75
|
experimental
| 22.373
| 0.18885
| 0.16001
|
Structure of human methionine aminopeptidase-2 complexed with spiroepoxytriazole inhibitor (+)-31a
|
GPKVQTDPPSVPICDLYPNGVFPKGQECEYPPTQDGRTAAWRTTSEEKKALDQASEEIWNDFREAAEAHRQVRKYVMSWIKPGMTMIEICEKLEDCSRKLIKENGLNAGLAFPTGCSLNNCAAHYTPNAGDTTVLQYDDICKIDFGTHISGRIIDCAFTVTFNPKYDTLLKAVKDATNTGIKCAGIDVRLCDVGEAIQEVMESYEVEIDGKTYQVKPIRNLNGHSIGQYRIHAGKTVPIVKGGEATRMEEGEVYAIETFGSTGKGVVHDDMECSHYMKNFDVGHVPIRLPRTKHLLNVINENFGTLAFCRRWLDRLGESKYLMALKNLCDLGIVDPYPPLCDIKGSYTAQFEHTILLRPTCKEVVSRGDDY
|
Protein
| 371
|
polypeptide(L)
| 1
| 41.51
|
Methionine aminopeptidase 2
|
3.4.11.18
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 371
| 1
| 1
| 1
|
Monomer
|
A1
|
DMS
|
C2 H6 O S
| 78.133
|
DIMETHYL SULFOXIDE
|
InChI=1S/C2H6OS/c1-4(2)3/h1-2H3
|
CS(=O)C
| null | 8,331
|
5FDC
|
X-RAY DIFFRACTION
| 2.08
| 40.81
|
VAPOR DIFFUSION, HANGING DROP
| null |
2.5 M ammonium sulphate, 0.3 M sodium chloride, 0.1 M Tris-HCl, pH 8.4 and 5 mM 4-(hydroxymercurybenzoate)
| 293
|
2015-12-16
|
2016-05-18
| 2,384
| 1
| 260
| 264
| null | 30.03
| 1
|
1.75
|
experimental
| null | 0.204
| 0.17
|
Crystal structure of Human Carbonic Anhydrase II in complex with the anticonvulsant sulfamide JNJ-26990990 and its S,S-dioxide analog.
|
MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Protein
| 260
|
polypeptide(L)
| 1
| 29.289
|
Carbonic anhydrase 2
|
4.2.1.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 260
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 1,047
|
5LAB
|
X-RAY DIFFRACTION
| 2.26
| 45.26
|
VAPOR DIFFUSION, SITTING DROP
| 8
|
Tris, PEG6000, NNGH, pH 8.0, VAPOR DIFFUSION, SITTING DROP, temperature 293K
| 293
|
2016-06-14
|
2016-08-10
| 1,508
| 1
| 159
| 236
| null | 18.18
| 1
|
1.34
|
experimental
| 21.754
| 0.1945
| 0.15515
|
Crystal structure of the catalytic domain of human MMP12 complexed with the inhibitor NNGH
|
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG
|
Protein
| 159
|
polypeptide(L)
| 1
| 17.616
|
Macrophage metalloelastase
|
3.4.24.65
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 159
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 7,706
|
4YYP
|
X-RAY DIFFRACTION
| 3.68
| 66.64
|
VAPOR DIFFUSION, SITTING DROP
| null |
Thin needles grew in precipitant solution containing 100 mM Hepes, pH 7.0, 20 mM MgCl2 and 22% Poly(acrylic acid sodium salt) 5100. After extensive optimization and seeding plate-like crystals were grown in a drop consisting of 50% PLK4-PB3/STIL-CC complex solution, 33.3% precipitant solution (100 mM phosphate/citrate pH 4.2, 40% (v/v) Ethanol, 5% (w/v) PEG 1000) and 16.7% of seed stock solution.
| 291
|
2015-03-24
|
2015-07-29
| 967
| 2
| 119
| 15
| null | 13.45
| 2
|
2.6
|
experimental
| 89.61
| 0.2542
| 0.2174
|
Crystal structure of human PLK4-PB3 in complex with STIL-CC
|
SAQLLKSVFVKNVGWATQLTSGAVWVQFNDGSQLVVQAGVSSISYTSPNGQTTRYGENEKLPDYIKQKLQCLSSILLMFSNPTPNFH
|
Protein
| 87
|
polypeptide(L)
| 1
| 9.573
|
Serine/threonine-protein kinase PLK4
|
2.7.11.21
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 119
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
CL
|
Cl
| 35.453
|
CHLORIDE ION
|
InChI=1S/ClH/h1H/p-1
|
[Cl-]
| null | 7,563
|
8Q69
|
X-RAY DIFFRACTION
| 2.12
| 41.9
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
0.1 M MES pH 6.3-6.9, 50 mM Na2SO4, 18-25 % PEG 6000
| 290
|
2023-08-11
|
2024-08-21
| 4,919
| 2
| 552
| 405
| null | 66.81
| 1
|
1.96
|
experimental
| null | 0.2892
| 0.2423
|
Crystal structure of HsRNMT complexed with inhibitor DDD1060606
|
SQSRIFYLRNFNNWMKSVLIGEFLEKVRQKKKRDITVLDLGCGKGGDLLKWKKGRINKLVCTDIADVSVKQCQQRYEDMKNRRDSEYIFSAEFITADSSKELLIDKFRDPQMCFDICSCQFVCHYSFESYEQADMMLRNACERLSPGGYFIGTTPNSFELIRRLEASETESFGNEIYTVKFQKKGDYPLFGCKYDFNLEGVVDVPEFLVYFPLLNEMAKKYNMKLVYKKTFLEFYEEKIKNNENKMLLKRMGLGCLSKSEWEATSIYLVFAFEKQQ
|
Protein
| 276
|
polypeptide(L)
| 2
| 32.551
|
mRNA cap guanine-N7 methyltransferase
|
2.1.1.56
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 276
| 1
| 1
| 1
|
Monomer
|
A1
|
SAH
|
C14 H20 N6 O5 S
| 384.411
|
S-ADENOSYL-L-HOMOCYSTEINE
|
InChI=1S/C14H20N6O5S/c15-6(14(23)24)1-2-26-3-7-9(21)10(22)13(25-7)20-5-19-8-11(16)17-4-18-12(8)20/h4-7,9-10,13,21-22H,1-3,15H2,(H,23,24)(H2,16,17,18)/t6-,7+,9+,10+,13+/m0/s1
|
c1nc(c2c(n1)n(cn2)C3C(C(C(O3)CSCCC(C(=O)O)N)O)O)N
|
Y
| 2,815
|
6BH3
|
X-RAY DIFFRACTION
| 2.24
| 45.17
|
VAPOR DIFFUSION, SITTING DROP
| null |
1.2-1.35 M (NH4)2SO4, 0.1 M Tris-HCl (pH 8.6-9.2), 0-20% glycerol, 25 mM (Na/K) dibasic/monobasic phosphate
| 289
|
2017-10-29
|
2018-03-28
| 2,654
| 1
| 330
| 226
| null | 38.86
| 1
|
1.701
|
experimental
| null | 0.2157
| 0.1947
|
LINKED KDM5A JMJ DOMAIN BOUND TO THE INHIBITOR (S)-N-(1-(3-isopropyl-1H-pyrazole-5-carbonyl)pyrrolidin-3-yl)cyclopropanecarboxamide (Compound N55)
|
HNMAGVGPGGYAAEFVPPPECPVFEPSWEEFTDPLSFIGRIRPLAEKTGICKIRPPKDWQPPFACEVKSFRFTPRVQRLNELEAMTRVRPREAFGFEQAVREYTLQSFGEMADNFKSDYFNMPVHMVPTELVEKEFWRLVSSIEEDVIVEYGADISSKDFGSGFPVKDGRRKILPEEEEYALSGWNLNNMPVLEQSVLAHINVDISGMKVPWLYVGMCFSSFCWHIEDHWSYSINYLHWGEPKTWYGVPSHAAEQLEEVMRELAPELFESQPDLLHQLVTIMNPNVLMEHGVPVYRTNQCAGEFVVTFPRAYHSGFNQGYNFAEAVNFCT
|
Protein
| 330
|
polypeptide(L)
| 1
| 37.945
|
Lysine-specific demethylase 5A, linked KDM5A JMJ domain
|
1.14.11
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 330
| 1
| 1
| 1
|
Monomer
|
A1
|
DQJ
|
C15 H22 N4 O2
| 290.361
|
N-{(3S)-1-[5-(propan-2-yl)-1H-pyrazole-3-carbonyl]pyrrolidin-3-yl}cyclopropanecarboxamide
|
InChI=1S/C15H22N4O2/c1-9(2)12-7-13(18-17-12)15(21)19-6-5-11(8-19)16-14(20)10-3-4-10/h7,9-11H,3-6,8H2,1-2H3,(H,16,20)(H,17,18)/t11-/m0/s1
|
CC(C)c1cc(n[nH]1)C(=O)N2CCC(C2)NC(=O)C3CC3
|
Y
| 8,161
|
5OS0
|
X-RAY DIFFRACTION
| 2.79
| 55.84
|
VAPOR DIFFUSION, SITTING DROP
| 8.5
|
0.1 M Tris, pH 8.5: 0.5 M NaCl: 0.2 M MgCl2: 32.5 % v/v PEG 3350
| 298
|
2017-08-16
|
2017-11-01
| 2,333
| 1
| 265
| 141
| null | 31.51
| 1
|
1.74
|
experimental
| 43.1512
| 0.2635
| 0.2173
|
Crystal structure of Aurora-A kinase in complex with an allosterically binding fragment
|
QWALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRTTLAGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWITANSSKPS
|
Protein
| 265
|
polypeptide(L)
| 1
| 30.798
|
Aurora kinase A
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 265
| 1
| 1
| 1
|
Monomer
|
A1
|
MG
|
Mg
| 24.305
|
MAGNESIUM ION
|
InChI=1S/Mg/q+2
|
[Mg+2]
| null | 9,936
|
4WZX
|
X-RAY DIFFRACTION
| 2.19
| 43.83
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
50mM MES pH 6.5, 5mM Cobalt chloride, 800mM ammonium sulfate
| 295
|
2014-11-20
|
2015-06-03
| 896
| 2
| 118
| 69
| null | 13.44
| 2
|
1.3859
|
experimental
| null | 0.18
| 0.1513
|
ULK3 regulates cytokinetic abscission by phosphorylating ESCRT-III proteins
|
GPHMGTSARDLLREMARDKPRLLAALEVASAAMAKEEAAGGEQDALDLYQHSLGELLLLLAAEPPGRRRELLHTEVQNLMARAEYLKEQVKMRES
|
Protein
| 95
|
polypeptide(L)
| 1
| 10.551
|
Serine/threonine-protein kinase ULK3
|
2.7.11.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 118
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
CO
|
Co
| 58.933
|
COBALT (II) ION
|
InChI=1S/Co/q+2
|
[Co+2]
| null | 2,320
|
5RYC
|
X-RAY DIFFRACTION
| 2.1
| 41.44
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
30 mM sodium nitrate, 30 mM dibasic sodium phosphate, 30 mM ammonium sulfate, 100 mM MES/imidazole, pH 6.5, 20% PEG500 MME, 10% PEG20000
| 293
|
2020-10-30
|
2020-11-11
| 4,790
| 1
| 463
| 441
| null | 53.28
| 1
|
1.56
|
experimental
| 18.459
| 0.2051
| 0.174
|
INPP5D PanDDA analysis group deposition -- Crystal Structure of the phosphatase and C2 domains of SHIP1 in complex with Z18197050
|
SMEQPEPDMITIFIGTWNMGNAPPPKKITSWFLSKGQGKTRDDSADYIPHDIYVIGTQEDPLSEKEWLEILKHSLQEITSVTFKTVAIHTLWNIRIVVLAKPEHENRISHICTDNVKTGIANTLGNKGAVGVSFMFNGTSLGFVNSHLTSGSEKKLRRNQNYMNILRFLALGDKKLSPFNITHRFTHLFWFGDLNYRVDLPTWEAETIIQKIKQQQYADLLSHDQLLTERREQKVFLHFEEEEITFAPTYRFERLTRDKYAYTKQKATGMKYNLPSWCDRVLWKSYPLVHVVCQSYGSTSDIMTSDHSPVFATFEAGVTSQFVSKNGPGTVDSQGQIEFLRCYATLKTKSQTKFYLEFHSSCLESFVKSQEGENEEGSEGELVVKFGETLPKLKPIISDPEYLLDQHILISIKSSDSDESYGEGCIALRLEATETQLPIYTPLTHHGELTGHFQGEIKLQTSQ
|
Protein
| 463
|
polypeptide(L)
| 1
| 52.878
|
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 1
|
3.1.3.86
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 463
| 1
| 1
| 1
|
Monomer
|
A1
|
WL1
|
C8 H8 O2 S
| 168.213
|
methyl 4-sulfanylbenzoate
|
InChI=1S/C8H8O2S/c1-10-8(9)6-2-4-7(11)5-3-6/h2-5,11H,1H3
|
COC(=O)c1ccc(cc1)S
| null | 8,268
|
6HWO
|
X-RAY DIFFRACTION
| 2.62
| 53.1
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
24% PEG 3350, 30% Ethylene Glycol, 0.1 M HEPES pH 7.5
| 293
|
2018-10-12
|
2019-07-24
| 11,546
| 4
| 1,456
| 590
| null | 174.3
| 1
|
1.99
|
experimental
| 43.247
| 0.25539
| 0.19819
|
Crystal structure of human phosphodiesterase 4D2 catalytic domain with inhibitor NPD-1335
|
GSHMIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTL
|
Protein
| 364
|
polypeptide(L)
| 4
| 41.808
|
cAMP-specific 3',5'-cyclic phosphodiesterase 4D
|
3.1.4.53
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 364
| 1
| 1
| 1
|
Monomer
|
A1
|
PEG
|
C4 H10 O3
| 106.12
|
DI(HYDROXYETHYL)ETHER
|
InChI=1S/C4H10O3/c5-1-3-7-4-2-6/h5-6H,1-4H2
|
C(COCCO)O
| null | 9,696
|
8YGZ
|
X-RAY DIFFRACTION
| 2.5
| 50.83
|
VAPOR DIFFUSION, SITTING DROP
| null |
0.2M Li2SO4, 0.1M Tris-HCl pH8.5, 30% PEG4,000
| 293
|
2024-02-27
|
2024-03-13
| 2,542
| 1
| 314
| 176
| null | 36.31
| 1
|
2.1
|
experimental
| 44.21
| 0.254
| 0.1949
|
The Crystal Structure of TGF beta R2 kinase domain from Biortus.
|
GHNTELLPIELDTLVGKGRFAEVYKAKLKQNTSEQFETVAVKIFPYEEYASWKTEKDIFSDINLKHENILQFLTAEERKTELGKQYWLITAFHAKGNLQEYLTRHVISWEDLRKLGSSLARGIAHLHSDHTPCGRPKMPIVHRDLKSSNILVKNDLTCCLCDFGLSLRLDPTLSVDDLANSGQVGTARYMAPEVLASAMNLENVESFKQTDVYSMALVLWEMTSRCNAVGEVKDYEPPFGSKVREHPCVASMADNVLADAGRPEIPSFWLNHQGIQMVCETLTECWDHDPEARLTAQCVAERFSELEHLDRLSG
|
Protein
| 314
|
polypeptide(L)
| 1
| 35.587
|
TGF-beta receptor type-2
|
2.7.11.30
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 314
| 1
| 1
| 1
|
Monomer
|
A1
|
EDO
|
C2 H6 O2
| 62.068
|
1,2-ETHANEDIOL
|
InChI=1S/C2H6O2/c3-1-2-4/h3-4H,1-2H2
|
C(CO)O
|
Y
| 11,565
|
4XQ8
|
X-RAY DIFFRACTION
| 2.58
| 52.27
|
VAPOR DIFFUSION
| null |
0.1 M Lithium Sulfate monohydrate, 0.1 M HEPES-Sodium, 0.1 M Potassium Sodium Tartrate
| 277
|
2015-01-19
|
2016-02-24
| 4,236
| 4
| 680
| 99
| 1
| 78.83
| 1
|
2.798
|
experimental
| null | 0.2399
| 0.1817
|
Human DNA polymerase lambda- MgdATP binary complex and complex with 6 paired DNA
|
AQPSSQKATNHNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVTSYQEACSIPGIGKRMAEKIIEILESGHLRKLDHISESVPVLELFSNIWGAGTKTAQMWYQQGFRSLEDIRSQASLTTQQAIGLKHYSDFLERMPREEATEIEQTVQKAAQAFNSGLLCVACGSYRRGKATCGDVDVLITHPDGRSHRGIFSRLLDSLRQEGFLTDDLVSQEENGQQQKYLGVCRLPGPGRRHRRLDIIVVPYSEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSTAVVRNTHGCKVGPGRVLPTPTEKDVFRLLGLPYREPAERDW
|
Protein
| 334
|
polypeptide(L)
| 2
| 37.349
|
DNA polymerase lambda
|
2.7.7.7
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 346
| 3
| 3
| 1
|
Monomer
|
A1
|
DTP
|
C10 H16 N5 O12 P3
| 491.182
|
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE
|
InChI=1S/C10H16N5O12P3/c11-9-8-10(13-3-12-9)15(4-14-8)7-1-5(16)6(25-7)2-24-29(20,21)27-30(22,23)26-28(17,18)19/h3-7,16H,1-2H2,(H,20,21)(H,22,23)(H2,11,12,13)(H2,17,18,19)/t5-,6+,7+/m0/s1
|
c1nc(c2c(n1)n(cn2)C3CC(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)N
| null | 3,386
|
6TUH
|
X-RAY DIFFRACTION
| 2.23
| 44.92
|
VAPOR DIFFUSION, SITTING DROP
| 8.5
|
0.1 M TRIS 8.5 pH, 32.5% w/v PEG 3350, 200mM MgCl2
| 298
|
2020-01-07
|
2020-11-25
| 5,181
| 4
| 676
| 80
| 2
| 80.98
| 1
|
2.25
|
experimental
| 71.72
| 0.276
| 0.236
|
The PH domain of Bruton's tyrosine kinase mutant R28C
|
AAVILESIFLKRSQQKKKTSPLNFKKRLFLLTVHKLSYYEYDFERGRRGSKKGSIDVEKITCVETVVPEKNPPPERQIPRRGEESSEMEQISIIERFPYPFQVVYDEGPLYVFSPTEELRKRWIHQLKNVIRYNSDLVQKYHPSFWIDGQYLCCSQTAKNAMGCQILEN
|
Protein
| 169
|
polypeptide(L)
| 4
| 19.967
|
Tyrosine-protein kinase BTK
|
2.7.10.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 169
| 1
| 1
| 1
|
Monomer
|
A1
|
NXT
|
C9 H10 O3
| 166.174
|
4,5,6,7-tetrahydro-1-benzofuran-3-carboxylic acid
|
InChI=1S/C9H10O3/c10-9(11)7-5-12-8-4-2-1-3-6(7)8/h5H,1-4H2,(H,10,11)
|
c1c(c2c(o1)CCCC2)C(=O)O
|
Y
| 10,375
|
4WMA
|
X-RAY DIFFRACTION
| 2.46
| 50.03
|
VAPOR DIFFUSION, HANGING DROP
| 6.5
|
0.2 M Li2SO4, 0.1 M Bis-Tris, and 21% PEG3350
| 293
|
2014-10-08
|
2015-09-30
| 2,905
| 2
| 356
| 135
| 5
| 42.04
| 2
|
1.62
|
experimental
| 31.982
| 0.24252
| 0.21914
|
Crystal structure of mouse Xyloside xylosyltransferase 1 complexed with manganese,acceptor ligand and UDP-Glucose
|
SLEGGVVVPVDYHLLMMFTKAEHNAPLQAKARVALSSLLRLAKFEAHEVLNLHFVSEEASREVAKALLRELLPPAAGFKCKVIFHDVAVLTDKLFPVVEAMQKYFSAGSGTYYSDSIFFLSVAMHQIMPKEIPRIIQLDLDLKYKTNIRELFEEFDNFLPGAVIGIAREMQPVYRHTFWQFRHENPKTRVGDPPPEGLPGFNSGVMLLNLEAMRQSPLYSHLLEPSWVQQLADKYHFRGHLGDQDFFTMIGMEHPELFHVLDCTWNRQLCTWWRDHGYSDVFQAYFRCEGHVKIYHGNCNTPIPED
|
Protein
| 306
|
polypeptide(L)
| 1
| 35.295
|
Xyloside xylosyltransferase 1
|
2.4.2
|
PDB Primary Data
|
Mus musculus
| 10,090
| 356
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
MN
|
Mn
| 54.938
|
MANGANESE (II) ION
|
InChI=1S/Mn/q+2
|
[Mn+2]
| null | 766
|
5OVX
|
X-RAY DIFFRACTION
| 2.53
| 51.29
|
VAPOR DIFFUSION, HANGING DROP
| null |
26-28% PEG3350, 0.1M Bis-Tris pH5.5, 0.2M Lithium sulfate
| 277
|
2017-08-30
|
2017-11-22
| 2,617
| 1
| 305
| 252
| null | 35.66
| 1
|
2.1
|
experimental
| 27.5
| 0.228
| 0.1954
|
X-Ray Characterization of Striatal-Enriched Protein Tyrosine Phosphatase Inhibitors
|
MHHHHHHSSGVDLGTENLYFQSMSRVLQAEELHEKALDPFLLQAEFFEIPMNFVDPKEYDIPGLVRKNRYKTILPNPHSRVCLTSPDPDDPLSSYINANYIRGYGGEEKVYIATQGPIVSTVADFWRMVWQEHTPIIVMITNIEEMNEKCTEYWPEEQVAYDGVEITVQKVIHTEDYRLRLISLKSGTEERGLKHYWFTSWPDQKTPDRAPPLLHLVREVEEAAQQEGPHCAPIIVHCSAGIGRTGCFIATSICCQQLRQEGVVDILKTTCQLRQDRGGMIQTCEQYQFVHHVMSLYEKQLSHQS
|
Protein
| 305
|
polypeptide(L)
| 1
| 35.221
|
Tyrosine-protein phosphatase non-receptor type 5
|
3.1.3.48
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 305
| 1
| 1
| 1
|
Monomer
|
A1
|
AY5
|
C20 H17 Cl2 O5 P
| 439.226
|
[(~{S})-[4-[3-[(~{S})-(3,4-dichlorophenyl)-oxidanyl-methyl]phenyl]phenyl]-oxidanyl-methyl]phosphonic acid
|
InChI=1S/C20H17Cl2O5P/c21-17-9-8-16(11-18(17)22)19(23)15-3-1-2-14(10-15)12-4-6-13(7-5-12)20(24)28(25,26)27/h1-11,19-20,23-24H,(H2,25,26,27)/t19-,20-/m0/s1
|
c1cc(cc(c1)C(c2ccc(c(c2)Cl)Cl)O)c3ccc(cc3)C(O)P(=O)(O)O
| null | 2,861
|
6I0B
|
X-RAY DIFFRACTION
| 3.1
| 60.38
|
VAPOR DIFFUSION, HANGING DROP
| null |
MES pH 6.5
Ammonium Sulphate
| 293
|
2018-10-25
|
2019-03-27
| 4,566
| 1
| 529
| 114
| 3
| 63.29
| 1
|
2.384
|
experimental
| null | 0.2439
| 0.1892
|
Human butyrylcholinesterase in complex with the S enantiomer of a chlorotacrine-tryptophan multi-target inhibitor.
|
EDDIIIATKNGKVRGMQLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVYGAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDVVGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLERRDQYTKAEEILSRSIVKRWANFAKYGNPQETQNQSTSWPVFKSTEQKYLTLNTESTRIMTKLRAQQCRFWTSFFPKV
|
Protein
| 529
|
polypeptide(L)
| 1
| 59.714
|
Cholinesterase
|
3.1.1.8
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 529
| 1
| 1
| 1
|
Monomer
|
A1
|
NAG
|
C8 H15 N O6
| 221.208
|
2-acetamido-2-deoxy-beta-D-glucopyranose
|
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
|
CC(=O)NC1C(C(C(OC1O)CO)O)O
| null | 5,860
|
8I1J
|
X-RAY DIFFRACTION
| 1.83
| 32.82
|
VAPOR DIFFUSION, HANGING DROP
| null |
sodium citrate, caps, NaCl
| 293
|
2023-01-13
|
2023-03-22
| 3,186
| 2
| 312
| 334
| 1
| 37.19
| 1
|
1.08
|
experimental
| 20.24
| 0.1742
| 0.1418
|
Crystal structure of human MTH1(G2K/D120N mutant) in complex with 2-oxo-dATP at pH 9.7
|
MKASRLYTLVLVLQPQRVLLGMKKRGFGAGRWNGFGGKVQEGETIEDGARRELQEESGLTVDALHKVGQIVFEFVGEPELMDVHVFCTDSIQGTPVESDEMRPCWFQLDQIPFKDMWPDNSYWFPLLLQKKKFHGYFKFQGQDTILDYTLREVDTV
|
Protein
| 156
|
polypeptide(L)
| 2
| 18.043
|
7,8-dihydro-8-oxoguanine triphosphatase
|
3.6.1.55
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 156
| 1
| 1
| 1
|
Monomer
|
A1
|
6U4
|
C10 H16 N5 O13 P3
| 507.181
|
[[(2R,3S,5R)-5-(6-azanyl-2-oxidanylidene-1H-purin-9-yl)-3-oxidanyl-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] phosphono hydrogen phosphate
|
InChI=1S/C10H16N5O13P3/c11-8-7-9(14-10(17)13-8)15(3-12-7)6-1-4(16)5(26-6)2-25-30(21,22)28-31(23,24)27-29(18,19)20/h3-6,16H,1-2H2,(H,21,22)(H,23,24)(H2,18,19,20)(H3,11,13,14,17)/t4-,5+,6+/m0/s1
|
C1C(C(OC1N2C=NC3=C(NC(=O)N=C32)N)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O
|
Y
| 3,844
|
7SUY
|
X-RAY DIFFRACTION
| 2.1
| 41.52
|
VAPOR DIFFUSION, HANGING DROP
| 7.8
|
1.6 M sodium citrate, 50 mM tris base
| 293
|
2021-11-18
|
2022-04-06
| 2,284
| 1
| 257
| 198
| null | 29.37
| 1
|
1.405
|
experimental
| 19.3444
| 0.1873
| 0.1653
|
Carbonic Anhydrase IX-mimic Complexed with 2-((3-Aminopropyl)(phenethyl)amino)-N-(4-fluorobenzyl)-N-(4-sulfamoylphenethyl)acetamide
|
HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHSFQVTFDDSQDKAVLKGGPLDGTYRLLQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDVGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVLDSIKTEGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLAECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDNWRPAQPLKNRQIKASFK
|
Protein
| 257
|
polypeptide(L)
| 1
| 28.844
|
Carbonic anhydrase 2
|
4.2.1.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 257
| 1
| 1
| 1
|
Monomer
|
A1
|
C97
|
C15 H19 N3 O4 S
| 337.394
|
N-[(furan-2-yl)methyl]-N-[2-(4-sulfamoylphenyl)ethyl]glycinamide
|
InChI=1S/C15H19N3O4S/c16-10-15(19)18(11-13-2-1-9-22-13)8-7-12-3-5-14(6-4-12)23(17,20)21/h1-6,9H,7-8,10-11,16H2,(H2,17,20,21)
|
c1cc(oc1)CN(CCc2ccc(cc2)S(=O)(=O)N)C(=O)CN
|
Y
| 1,144
|
7GSZ
|
X-RAY DIFFRACTION
| 3.39
| 63.77
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
0.3 M magnesium acetate, 0.1 M HEPES pH 7.5, 0.1% beta-mercaptoethanol, 13-14% PEG 8000, 2% ethanol
| 277
|
2024-01-03
|
2024-01-24
| 2,556
| 1
| 321
| 245
| null | 37.67
| 1
|
1.91
|
experimental
| 44.292
| 0.2409
| 0.1996
|
PanDDA Analysis group deposition -- Crystal structure of PTP1B in complex with FMSOA000686b
|
MEMEKEFEQIDKSGSWAAIYQDIRHEASDFPSRVAKLPKNKNRNRYRDVSPFDHSRIKLHQEDNDYINASLIKMEEAQRSYILTQGPLPNTVGHFWEMVWEQKSRGVVMLNRVMEKGSLKCAQYWPQKEEKEMIFEDTNLKLTLISEDIKSYYTVRQLELENLTTQETREILHFHYTTWPDFGVPESPASFLNFLFKVRESGSLSPEHGPVVVHCSAGIGRSGTFCLADTCLLLMDKRKDPSSVDIKKVLLEMRKFRMGLIQTADQLRFSYLAVIEGAKFIMGDSSVQDQWKELSHEDLEPPPEHIPPPPRPPKRILEPHN
|
Protein
| 321
|
polypeptide(L)
| 1
| 37.346
|
Tyrosine-protein phosphatase non-receptor type 1
|
3.1.3.48
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 321
| 1
| 1
| 1
|
Monomer
|
A1
|
TRS
|
C4 H12 N O3
| 122.143
|
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL
|
InChI=1S/C4H11NO3/c5-4(1-6,2-7)3-8/h6-8H,1-3,5H2/p+1
|
C(C(CO)(CO)[NH3+])O
| null | 9,757
|
5B6C
|
X-RAY DIFFRACTION
| 2.33
| 47.18
|
VAPOR DIFFUSION, HANGING DROP
| 7.5
|
21%(w/v) PEG 8000, 2.9mM n-nonyl-beta-thiomaltoside, 0.1M HEPES, pH 7.5
| 293.15
|
2016-05-26
|
2017-01-04
| 1,740
| 2
| 185
| 274
| null | 20.94
| 2
|
1.55
|
experimental
| 17.623
| 0.1995
| 0.15797
|
Structural Details of Ufd1 binding to p97
|
GSNRPNRLIVDEAINEDNSVVSLSQPKMDELQLFRGDTVLLKGKKRREAVCIVLSDDTCSDEKIRMNRVVRNNLRVRLGDVISIQPCPDVKYGKRIHVLPIDDTVEGITGNLFEVYLKPYFLEAYRPIRKGDIFLVRGGMRAVEFKVVETDPSPYCIVAPDTVIHCEGEPIKRA
|
Protein
| 174
|
polypeptide(L)
| 1
| 19.726
|
Transitional endoplasmic reticulum ATPase
|
3.6.4.6
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 185
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
| null | null | null | null | null | null | null | 9,671
|
7MHD
|
X-RAY DIFFRACTION
| 1.97
| 37.64
|
VAPOR DIFFUSION, SITTING DROP
| null |
0.3 ul of 8 mg/ml FASN-TE in 100 mM NaCl, 50 mM BisTris pH 6.0, 10 mM DTT, 0.5 mM of the inhibitor and 1% DMSO were mixed with 0.2 ul of well solution 10% PEG400, 50 mM TRIS-Cl pH 8.5, 1 mM DTT, 1 mM Ethylenediaminetetraacetic acid disodium salt (EDTA), 300 mM NaCl.
| 293
|
2021-04-15
|
2022-04-20
| 2,374
| 1
| 298
| 106
| null | 32.93
| 1
|
2.03
|
experimental
| 42.494
| 0.2457
| 0.1928
|
Thioesterase Domain of Human Fatty Acid Synthase (FASN-TE) binding a competitive inhibitor SBP-7635
|
GSGGGGGSTQLNLRSLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLDSIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGSPTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAAVDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGADYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEH
|
Protein
| 298
|
polypeptide(L)
| 1
| 32.525
|
Fatty acid synthase
|
3.1.2.14
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 298
| 1
| 1
| 1
|
Monomer
|
A1
|
ZEP
|
C20 H21 F N2 O2 S2
| 404.521
|
N,N-diethyl-4-{2-[(2-fluorophenyl)methyl]-1,3-thiazol-4-yl}benzene-1-sulfonamide
|
InChI=1S/C20H21FN2O2S2/c1-3-23(4-2)27(24,25)17-11-9-15(10-12-17)19-14-26-20(22-19)13-16-7-5-6-8-18(16)21/h5-12,14H,3-4,13H2,1-2H3
|
CCN(CC)S(=O)(=O)c1ccc(cc1)c2csc(n2)Cc3ccccc3F
|
Y
| 2,510
|
5HYN
|
X-RAY DIFFRACTION
| 2.82
| 56.33
|
VAPOR DIFFUSION, SITTING DROP
| 6.5
|
25% PEG3350, 400mM Ammonian Citrate pH6.5
| 291
|
2016-02-01
|
2016-05-11
| 35,028
| 20
| 5,068
| null | null | 586.82
| 5
|
2.95
|
experimental
| null | 0.2733
| 0.2191
|
Structure of Human Polycomb Repressive Complex 2 (PRC2) with oncogenic histone H3K27M peptide
|
ATKAARMSAPATG
|
Protein
| 13
|
polypeptide(L)
| 4
| 1.234
|
H3K27M
| null | null |
Homo sapiens
| 9,606
| 1,267
| 5
| 5
| 1
|
Hetero 5-mer
|
A1, B1, C1, D1, E1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 10,332
|
8SWC
|
X-RAY DIFFRACTION
| 2.6
| 52.61
|
VAPOR DIFFUSION, HANGING DROP
| null |
2:1 complex : precipitant (0.1 M sodium acetate, pH 4.6, 8% w/v PEG4000), cryoprotection: mother liquor + 25% v/v glycerol, 1 minute
| 277
|
2023-05-18
|
2024-06-19
| 2,052
| 3
| 334
| 5
| null | 46.62
| 1
|
2.68
|
experimental
| 83.64
| 0.22
| 0.1915
|
RNase H complex with ASO (OOO) and RNA
|
HHHHHHHHMSWLLFLAHRVALAALPCRRGSRGFGMFYAVRRGRKTGVFLTWNECRAQVDRFPAARFKKFATEDEAWAFVRKSASPEVSEGHENQHGQESEAKASKRLREPLDGDGHESAEPYAKHMKPSVEPAPPVSRDTFSYMGDFVVVYTDGCCSSNGRRRPRAGIGVYWGPGHPLNVGIRLPGRQTNQRAEIHAACKAIEQAKTQNINKLVLYTNSMFTINGITNWVQGWKKNGWKTSAGKEVINKEDFVALERLTQGMDIQWMHVPGHSGFIGNEEADRLAREGAKQSED
|
Protein
| 294
|
polypeptide(L)
| 1
| 33.218
|
Ribonuclease H1
|
3.1.26.4
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 334
| 3
| 3
| 1
|
Monomer
|
A1
|
PO4
|
O4 P
| 94.971
|
PHOSPHATE ION
|
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
|
[O-]P(=O)([O-])[O-]
| null | 2,273
|
6EKN
|
X-RAY DIFFRACTION
| 2.16
| 43.15
|
VAPOR DIFFUSION, SITTING DROP
| 10
|
Protein: 1 micro-L MMP12 at 290 micro-M with 10 milli-M acetohydroxamate + 0.1 Micro-L BE6 from 10 milii-M in 100% DMSO
Precipitant: 17% PEG 20K, 250 milli-M NaCl, 100 milii-M TRIS HCl, pH 10.0.
cryoprotectant: 40% (25 % di-ethylene glycol + 25 % glycerol + 25 % 1,2-propanediol) 10 % PEG 10K, 200 milli-M NaCl, 100 milli-M AAB (Na acetate,N-(2-Acetamido)iminodiacetic acid (ADA), Bicine) 10% acid/90% basic
| 293
|
2017-09-26
|
2018-05-16
| 1,548
| 1
| 159
| 151
| null | 18.38
| 1
|
1.2
|
experimental
| 20.711
| 0.17523
| 0.1442
|
Crystal structure of MMP12 in complex with inhibitor BE7.
|
MGPVWRKHYITYRINNYTPDMNREDVDYAIRKAFQVWSNVTPLKFSKINTGMADILVVFARGAHGDDHAFDGKGGILAHAFGPGSGIGGDAHFDEDEFWTTHSGGTNLFLTAVHEIGHSLGLGHSSDPKAVMFPTYKYVDINTFRLSADDIRGIQSLYG
|
Protein
| 159
|
polypeptide(L)
| 1
| 17.616
|
Macrophage metalloelastase
|
3.4.24.65
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 159
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 5,767
|
5V05
|
X-RAY DIFFRACTION
| 2.65
| 53.52
|
VAPOR DIFFUSION, SITTING DROP
| 7
|
100 mM sodium acetate, pH 7.0, 10 mM potassium chloride, 2-4% PEG4000
| 290
|
2017-02-28
|
2017-05-24
| 3,253
| 3
| 381
| 54
| null | 47.48
| 1
|
2.902
|
experimental
| null | 0.2484
| 0.1992
|
Crystal structure of human exonuclease 1 Exo1 (WT) in complex with 5' recessed-end DNA (rIII)
|
MGIQGLLQFIKEASEPIHVRKYKGQVVAVDTYCWLHKGAIACAEKLAKGEPTDRYVGFCMKFVNMLLSHGIKPILVFDGCTLPSKKEVERSRRERRQANLLKGKQLLREGKVSEARECFTRSINITHAMAHKVIKAARSQGVDCLVAPYEADAQLAYLNKAGIVQAIITEDSDLLAFGCKKVILKMDQFGNGLEIDQARLGMCRQLGDVFTEEKFRYMCILSGCDYLSSLRGIGLAKACKVLRLANNPDIVKVIKKIGHYLKMNITVPEDYINGFIRANNTFLYQLVFDPIKRKLIPLNAYEDDVDPETLSYAGQYVDDSIALQIALGNKDINTFEQIDDYNPDTAMPAHSRENLYFQ
|
Protein
| 358
|
polypeptide(L)
| 1
| 40.355
|
Exonuclease 1
|
3.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 381
| 3
| 3
| 1
|
Monomer
|
A1
|
MN
|
Mn
| 54.938
|
MANGANESE (II) ION
|
InChI=1S/Mn/q+2
|
[Mn+2]
| null | 5,226
|
5F6V
|
X-RAY DIFFRACTION
| 2.71
| 54.63
|
VAPOR DIFFUSION, HANGING DROP
| 8.5
|
0.1M Tris pH 8.5, 8% (w/v) polyethylene glycol 8000
| 294
|
2015-12-07
|
2016-04-27
| 1,582
| 1
| 157
| 228
| null | 17.91
| 1
|
1.492
|
experimental
| null | 0.1838
| 0.1519
|
Crystal structure of Ubc9 (K48/K49A/E54A) complexed with Fragment 1 (biphenol from fragment cocktail screen)
|
SGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGAAGTPWAGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS
|
Protein
| 157
|
polypeptide(L)
| 1
| 17.725
|
SUMO-conjugating enzyme UBC9
|
6.3.2
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 157
| 1
| 1
| 1
|
Monomer
|
A1
|
5VL
|
C12 H10 O2
| 186.207
|
2-(2-hydroxyphenyl)phenol
|
InChI=1S/C12H10O2/c13-11-7-3-1-5-9(11)10-6-2-4-8-12(10)14/h1-8,13-14H
|
c1ccc(c(c1)c2ccccc2O)O
| null | 5,938
|
6QFE
|
X-RAY DIFFRACTION
| 2.97
| 58.59
|
VAPOR DIFFUSION, SITTING DROP
| 5.6
|
100mM Sodium Citrate pH 5.6, 20% PEG 4K, 5% Glycerol, 10% Iso-propanol
| 293
|
2019-01-10
|
2019-05-08
| 4,083
| 2
| 454
| 393
| 12
| 52.52
| 1
|
1.67
|
experimental
| 30.43
| 0.242
| 0.211
|
Crystal Structure of Human Kallikrein 5 in complex with GSK144
|
IINGSDCDMHTQPWQAALLLRPNQLYCGAVLVHPQWLLTAAHCRKKVFRVRLGHYSLSPVYESGQQMFQGVKSIPHPGYSHPGHSNDLMLIKLNRRIRPTKDVRPINVSSHCPSAGTKCLVSGWGTTKSPQVHFPKVLQCLNISVLSQKRCEDAYPRQIDDTMFCAGDKAGRDSCQGDSGGPVVCNGSLQGLVSWGDYPCARPNRPGVYTNLCKFTKWIQETIQANS
|
Protein
| 227
|
polypeptide(L)
| 2
| 25.193
|
Kallikrein-5
|
3.4.21
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 227
| 1
| 1
| 1
|
Monomer
|
A1
|
NAG
|
C8 H15 N O6
| 221.208
|
2-acetamido-2-deoxy-beta-D-glucopyranose
|
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
|
CC(=O)NC1C(C(C(OC1O)CO)O)O
| null | 10,458
|
6DKB
|
X-RAY DIFFRACTION
| 2.29
| 46.23
|
VAPOR DIFFUSION, SITTING DROP
| 8
|
Well volume: 30.0 uL
Drop volume from well: 0.2 uL
Drop protein volume: 0.4 uL
Well Ingredients:
Polymer: 10.0 %w/v (6.0 uL of stock 50.0 %w/v) PEG 3350
Buffer: 16.0 %v/v (4.8 uL of stock 100.0 %v/v) tacsimate (pH 8.00)
Organic (non-volatile): 10.0 %v/v (3.0 uL of stock 100.0 %v/v) Ethylene glycol
Additive: 0.025 M (1.5 uL of stock 0.5 M) TCEP hydrochloride
Plate setup temperature: 13 C
Plate incubation temperature: 21 C
| 294
|
2018-05-29
|
2018-07-11
| 2,222
| 1
| 320
| 1
| null | 36.63
| 1
|
2.68
|
experimental
| 80.37
| 0.245
| 0.2159
|
Crystal structure of Trk-A in complex with the Pan-Trk Kinase Inhibitor, compound 10b.
|
GSTEGKGSGLQGHIIENPQYFSDACVHHIKRRDIVLKWELGEGAFGKVFLAECHNLLPEQDKMLVAVKALKEASESARQDFQREAELLTMLQHQHIVRFFGVCTEGRPLLMVFEYMRHGDLNRFLRSHGPDAKLLAGGEDVAPGPLGLGQLLAVASQVAAGMVYLAGLHFVHRDLATRNCLVGQGLVVKIGDFGMSRDIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWYQLSNTEAIDCITQGRELERPRACPPEVYAIMRGCWQREPQQRHSIKDVHARLQALAQAPPVYLDVLG
|
Protein
| 320
|
polypeptide(L)
| 1
| 36.111
|
High affinity nerve growth factor receptor
|
2.7.10.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 320
| 1
| 1
| 1
|
Monomer
|
A1
|
FKY
|
C24 H23 F4 N5 O4
| 521.464
|
2-{[(3R,4S)-3-fluoro-1-{[4-(trifluoromethoxy)phenyl]acetyl}piperidin-4-yl]oxy}-5-(1-methyl-1H-imidazol-4-yl)pyridine-3-carboxamide
|
InChI=1S/C24H23F4N5O4/c1-32-12-19(31-13-32)15-9-17(22(29)35)23(30-10-15)36-20-6-7-33(11-18(20)25)21(34)8-14-2-4-16(5-3-14)37-24(26,27)28/h2-5,9-10,12-13,18,20H,6-8,11H2,1H3,(H2,29,35)/t18-,20+/m1/s1
|
Cn1cc(nc1)c2cc(c(nc2)OC3CCN(CC3F)C(=O)Cc4ccc(cc4)OC(F)(F)F)C(=O)N
| null | 6,112
|
6N2S
|
X-RAY DIFFRACTION
| 2.23
| 44.74
|
VAPOR DIFFUSION, SITTING DROP
| null |
16-18% PEG 2000 Monomethyl Ether
| 291
|
2018-11-14
|
2019-03-27
| 3,356
| 4
| 366
| 81
| null | 48.31
| 1
|
2.457
|
experimental
| 44.6413
| 0.2896
| 0.2024
|
Ternary complex crystal structure of DNA polymerase Beta with 5-carboxy-dC (5-caC) at the templating position
|
MSKRKAPQETLNGGITDMLTELANFEKNVSQAIHKYNAYRKAASVIAKYPHKIKSGAEAKKLPGVGTKIAEKIDEFLATGKLRKLEKIRQDDTSSSINFLTRVSGIGPSAARKFVDEGIKTLEDLRKNEDKLNHHQRIGLKYFGDFEKRIPREEMLQMQDIVLNEVKKVDSEYIATVCGSFRRGAESSGDMDVLLTHPSFTSESTKQPKLLHQVVEQLQKVHFITDTLSKGETKFMGVCQLPSKNDEKEYPHRRIDIRLIPKDQYYCGVLYFTGSDIFNKNMRAHALEKGFTINEYTIRPLGVTGVAGEPLPVDSEKDIFDYIQWKYREPKDRSE
|
Protein
| 335
|
polypeptide(L)
| 1
| 38.242
|
DNA polymerase beta
|
2.7.7.7
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 366
| 4
| 4
| 1
|
Monomer
|
A1
|
MG
|
Mg
| 24.305
|
MAGNESIUM ION
|
InChI=1S/Mg/q+2
|
[Mg+2]
| null | 102
|
8J7Q
|
X-RAY DIFFRACTION
| 2.76
| 55.44
|
VAPOR DIFFUSION
| null |
0.2 M (NH4)2SO4, 20% PEG8000, 100 mM MES PH6.0
| 289
|
2023-04-28
|
2024-04-03
| 2,249
| 1
| 289
| 196
| null | 32.55
| 1
|
1.69
|
experimental
| null | 0.2456
| 0.2155
|
The active site mutant of human inorganic pyrophosphatase
|
MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKGKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGANAAIAVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINVDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTLSESPFKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN
|
Protein
| 289
|
polypeptide(L)
| 1
| 32.547
|
Inorganic pyrophosphatase
|
3.6.1.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 289
| 1
| 1
| 1
|
Monomer
|
A1
| null | null | null | null | null | null | null | 1,989
|
4WLR
|
X-RAY DIFFRACTION
| 2.63
| 53.27
|
VAPOR DIFFUSION, SITTING DROP
| 6.6
|
25% PEG 3350, 220 mM MgCl2,100 mM Bis-Tris
| 277
|
2014-10-07
|
2015-03-04
| 3,920
| 3
| 506
| 201
| null | 56.83
| 3
|
1.997
|
experimental
| null | 0.2273
| 0.1806
|
Crystal Structure of mUCH37-hRPN13 CTD-hUb complex
|
MSSNAGEWCLMESDPGVFTELIKGFGCRGAQVEEIWSLEPESFEKLKPVHGLIFLFKWQPGEEPAGSVVQDSRLETIFFAKQVINNACATQAIVSVLLNCTHQDVHLGETLSEFKEFSQSFDAAMKGLALSNSDVIRQVHNSFARQQMFEFDTKTPAKEEDAFHFVSYVPVNGRLYELDGLREGPIDLGACNQDDWITAVRPVIEKRIQKYSEGEIRFNLMAIVSDRKMIYEQKIAELQRQLAEEPMDTDQGSTVLSAIQSEVARNQMLIEEEVQKLKRYKIENIRRKHNYLPFIMELLKTLAEHQQLIPLVEKAKEKQNAKKAQETK
|
Protein
| 328
|
polypeptide(L)
| 1
| 37.534
|
Ubiquitin carboxyl-terminal hydrolase isozyme L5
|
3.4.19.12
|
PDB Primary Data
|
Mus musculus
| 10,090
| 506
| 3
| 3
| 1
|
Hetero 3-mer
|
A1, B1, C1
| null | null | null | null | null | null | null | 6,832
|
7MNI
|
X-RAY DIFFRACTION
| 2.08
| 40.93
|
VAPOR DIFFUSION, HANGING DROP
| 8.3
|
20% w/v PEG4000, 0.22 M sodium chloride, 0.1 M Tris
| 294
|
2021-05-01
|
2022-06-15
| 9,442
| 4
| 1,294
| 418
| null | 143.79
| 2
|
2
|
experimental
| 61.7063
| 0.2084
| 0.1752
|
Crystal structure of the N-terminal domain of NUP88 in complex with NUP98 C-terminal Autoproteolytic Domain
|
SMAAAEGPVGDGELWQTWLPNHVVFLRLREGLKNQSPTEAEKPASSSLPSSPPPQLLTRNVVFGLGGELFLWDGEDSSFLVVRLRGPSGGGEEPALSQYQRLLCINPPLFEIYQVLLSPTQHHVALIGIKGLMVLELPKRWGKNSEFEGGKSTVNCSTTPVAERFFTSSTSLTLKHAAWYPSEILDPHVVLLTSDNVIRIYSLREPQTPTNVIILSEAEEESLVLNKGRAYTASLGETAVAFDFGPLAAVPKTLFGQNGKDEVVAYPLYILYENGETFLTYISLLHSPGNIGKLLGPLPMHPAAEDNYGYDACAVLCLPCVPNILVIATESGMLYHCVVLEGEEEDDHTSEKSWDSRIDLIPSLYVFECVELELALKLASGEDDPFDSDFSCPVKLHRDPKCPSRYHCTHEAGVHSVGLTWIHKLHKFLGSDEEDKDSLQELSTEQKCFVEHILCTKPLPCRQPAPIRGFWIVPDILGPTMICITSTYECLIWP
|
Protein
| 494
|
polypeptide(L)
| 2
| 54.635
|
Nuclear pore complex protein Nup88
| null | null |
Homo sapiens
| 9,606
| 647
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
| null | null | null | null | null | null | null | 4,639
|
6Q49
|
X-RAY DIFFRACTION
| 1.99
| 38.2
|
VAPOR DIFFUSION, HANGING DROP
| 7.4
|
10MG/ML CDK2 10% V/V PEG3350, 50 MM HEPES/NAOH, 50 MM NA/K PHOSPHATE, PH 7.5
| 293
|
2018-12-05
|
2019-03-20
| 2,771
| 1
| 306
| 305
| null | 35.01
| 1
|
1.0
|
experimental
| 23.835
| 0.19718
| 0.17524
|
CDK2 in complex with FragLite6
|
GPLGSPEFMENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL
|
Protein
| 306
|
polypeptide(L)
| 1
| 34.761
|
Cyclin-dependent kinase 2
|
2.7.11.22
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 306
| 1
| 1
| 1
|
Monomer
|
A1
|
DMS
|
C2 H6 O S
| 78.133
|
DIMETHYL SULFOXIDE
|
InChI=1S/C2H6OS/c1-4(2)3/h1-2H3
|
CS(=O)C
| null | 7,882
|
5L0S
|
X-RAY DIFFRACTION
| 2.41
| 49.04
|
VAPOR DIFFUSION, HANGING DROP
| 6.5
|
20% PEG5000 MME, 50 mM MES pH 6.5, 2mM CaCl2, 250mM NaCl, 5% glycerol
| 295
|
2016-07-28
|
2017-08-09
| 3,747
| 2
| 399
| 377
| 7
| 47.89
| 2
|
1.45
|
experimental
| 29.8733
| 0.1588
| 0.1394
|
human POGLUT1 in complex with Factor VII EGF1 and UDP
|
GSKWKVFIDQINRSLENYEPCSSQNCSCYHGVIEEDLTPFRGGISRKMMAEVVRRKLGTHYQITKNRLYRENDCMFPSRCSGVEHFILEVIGRLPDMEMVINVRDYPQVPKWMEPAIPVFSFSKTSEYHDIMYPAWTFWEGGPAVWPIYPTGLGRWDLFREDLVRSAAQWPWKKKNSTAYFRGSRTSPERDPLILLSRKNPKLVDAEYTKNQAWKSMKDTLGKPAAKDVHLVDHCKYKYLFNFRGVAASFRFKHLFLCGSLVFHVGDEWLEFFYPQLKPWVHYIPVKTDLSNVQELLQFVKANDDVAQEIAERGSQFIRNHLQMDDITCYWENLLSEYSKFLSYNVTRRKGYDQIIP
|
Protein
| 357
|
polypeptide(L)
| 1
| 42.077
|
Protein O-glucosyltransferase 1
|
2.4.1
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 399
| 2
| 2
| 1
|
Hetero 2-mer
|
A1, B1
|
NAG
|
C8 H15 N O6
| 221.208
|
2-acetamido-2-deoxy-beta-D-glucopyranose
|
InChI=1S/C8H15NO6/c1-3(11)9-5-7(13)6(12)4(2-10)15-8(5)14/h4-8,10,12-14H,2H2,1H3,(H,9,11)/t4-,5-,6-,7-,8-/m1/s1
|
CC(=O)NC1C(C(C(OC1O)CO)O)O
| null | 828
|
7JWE
|
X-RAY DIFFRACTION
| 2.32
| 46.95
|
VAPOR DIFFUSION, SITTING DROP
| 7.5
|
100 mM Tris pH 7.5, 250 mM (NH4)2SO4 and 20-22% PEG 4000
| 298
|
2020-08-25
|
2021-03-17
| 6,666
| 1
| 966
| 9
| null | 111.34
| 1
|
2.55
|
experimental
| 88.8962
| 0.2529
| 0.209
|
Gedatolisib bound to the PI3Kg catalytic subunit p110 gamma
|
MSEESQAFQRQLTALIGYDVTDVSNVHDDELEFTRRGLVTPRMAEVASRDPKLYAMHPWVTSKPLPEYLWKKIANNCIFIVIHRSTTSQTIKVSPDDTPGAILQSFFTKMAKKKSLMDIPESQSEQDFVLRVCGRDEYLVGETPIKNFQWVRHCLKNGEEIHVVLDTPPDPALDEVRKEEWPLVDDCTGVTGYHEQLTIHGKDHESVFTVSLWDCDRKFRVKIRGIDIPVLPRNTDLTVFVEANIQHGQQVLCQRRTSPKPFTEEVLWNVWLEFSIKIKDLPKGALLNLQIYCGKAPALSSKASAESPSSESKGKVQLLYYVNLLLIDHRFLLRRGEYVLHMWQISGKGEDQGSFNADKLTSATNPDKENSMSISILLDNYCHPIALPKHQPTPDPEGDRVRAEMPNQLRKQLEAIIATDPLNPLTAEDKELLWHFRYESLKHPKAYPKLFSSVKWGQQEIVAKTYQLLARREVWDQSALDVGLTMQLLDCNFSDENVRAIAVQKLESLEDDDVLHYLLQLVQAVKFEPYHDSALARFLLKRGLRNKRIGHFLFWFLRSEIAQSRHYQQRFAVILEAYLRGCGTAMLHDFTQQVQVIEMLQKVTLDIKSLSAEKYDVSSQVISQLKQKLENLQNSQLPESFRVPYDPGLKAGALAIEKCKVMASKKKPLWLEFKCADPTALSNETIGIIFKHGDDLRQDMLILQILRIMESIWETESLDLCLLPYGCISTGDKIGMIEIVKDATTIAKIQQSTVGNTGAFKDEVLNHWLKEKSPTEEKFQAAVERFVYSCAGYCVATFVLGIGDRHNDNIMITETGNLFHIDFGHILGNYKSFLGINKERVPFVLTPDFLFVMGTSGKKTSPHFQKFQDICVKAYLALRHHTNLLIILFSMMLMTGMPQLTSKEDIEYIRDALTVGKNEEDAKKYFLDQIEVCRDKGWTVQFNWFLHLVLGIKQGEKHSAHHHHHH
|
Protein
| 966
|
polypeptide(L)
| 1
| 110.727
|
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
|
2.7.1.153
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 966
| 1
| 1
| 1
|
Monomer
|
A1
|
VL1
|
C32 H41 N9 O4
| 615.726
|
Gedatolisib
|
InChI=1S/C32H41N9O4/c1-38(2)27-11-13-39(14-12-27)29(42)24-5-9-26(10-6-24)34-32(43)33-25-7-3-23(4-8-25)28-35-30(40-15-19-44-20-16-40)37-31(36-28)41-17-21-45-22-18-41/h3-10,27H,11-22H2,1-2H3,(H2,33,34,43)
|
CN(C)C1CCN(CC1)C(=O)c2ccc(cc2)NC(=O)Nc3ccc(cc3)c4nc(nc(n4)N5CCOCC5)N6CCOCC6
|
Y
| 8,627
|
4YPE
|
X-RAY DIFFRACTION
| 2.31
| 46.69
|
VAPOR DIFFUSION, SITTING DROP
| null |
PEG 3350, 20 mM Tris
| 277
|
2015-03-12
|
2015-09-02
| 3,572
| 2
| 452
| 107
| 2
| 53.24
| 1
|
2.2
|
experimental
| 32.169
| 0.2625
| 0.2165
|
ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM)
|
GAMAGSYKKIRSNVYVDVKPLSGYEATTCNCKKPDDDTRKGCVDDCLNRMIFAECSPNTCPCGEQCCNQRIQRHEWVQCLERFRAEEKGWGIRTKEPLKAGQFIIEYLGEVVSEQEFRNRMIEQYHNHSDFYCLNLDSGMVIDSYRMGNEARFINHSCDPNCEMQKWSVNGVYRIGLYALKDMPAGTELTYDYNFHSFNVEKQQLCKCGFEKCRGIIGGKSQRVNG
|
Protein
| 226
|
polypeptide(L)
| 2
| 26.026
|
Histone-lysine N-methyltransferase ASH1L
|
2.1.1.43
|
PDB Primary Data
|
Homo sapiens
| 9,606
| 226
| 1
| 1
| 1
|
Monomer
|
A1
|
ZN
|
Zn
| 65.409
|
ZINC ION
|
InChI=1S/Zn/q+2
|
[Zn+2]
| null | 1,672
|
End of preview. Expand
in Data Studio
Data Description
This dataset contains information about 11,832 human protein structures derived from the RCSB Protein Data Bank (PDB). It includes data on each structure's experimental method, crystallization conditions, molecular composition, and structural metrics.
Data Version and Change Log
Last Version: 1.0
Last Updated: May 18th, 2025
Data Steward and Owner
Data Steward: Satarupa Deb
Data Owner: RCSB Protein Data Bank
Tables
The dataset consists of three splits: train, test, and validation, stored in the data folder
Data:
Description: This table stores all information about different columns in the dataset.
Rows (total: 11832) correspond to individual protein structure entries, typically registered in the Protein Data Bank (PDB). Each row contains structural, chemical, and biological metadata about a single protein or protein-ligand complex.
Columns (total: 42) correspond to different observables or attributes of the protein structures
| Column Name | Data Type | Column Description |
|---|---|---|
| Entry ID | string | A unique identifier assigned to each protein structure in the Protein Data Bank. |
| Experimental Method | string | The technique used to determine the protein structure (e.g., X-ray diffraction, NMR). |
| Matthews Coefficient | float64 | A value that estimates the volume of a crystal occupied by the protein versus the solvent. |
| Percent Solvent Content | float64 | The percentage of solvent (usually water) present in the crystal structure. |
| Crystallization Method | string | The technique used to grow the crystals used for structure determination (e.g., vapor diffusion). |
| pH | float64 | The acidity or alkalinity level at which the crystallization was performed. |
| Crystal Growth Procedure | string | The detailed steps followed to grow the crystals used for structure determination. |
| Temp (K) | float64 | The temperature, measured in Kelvin, at which the crystallization experiment was conducted. |
| Deposition Date | string | The date when the protein structure was submitted to the Protein Data Bank. |
| Release Date | string | The date when the structure became publicly available in the PDB. |
| Number of Non-Hydrogen Atoms per Deposited Model | float64 | The count of non-hydrogen atoms present in the deposited protein structure. |
| Total Number of Polymer Instances (Chains) | float64 | The number of unique chains or instances of polymers present in the structure. |
| Total Number of Polymer Residues per Deposited Model | float64 | The total number of amino acid residues present in the protein model. |
| Number of Water Molecules per Deposited Model | float64 | The total number of water molecules present in the structure. |
| Disulfide Bond Count per Deposited Model | float64 | The number of disulfide bonds (covalent bonds between cysteine residues) in the protein structure. |
| Molecular Weight per Deposited Model | float64 | The molecular weight of the entire protein structure, including all chains. |
| Number of Distinct Protein Entities | float64 | The number of unique protein entities present in the structure. |
| Refinement Resolution (Å) | string | The resolution of the X-ray diffraction experiment, indicating the level of detail (in Ångströms). |
| Structure Determination Methodology | string | The overall approach or methodology used to solve the protein structure. |
| Average B Factor | float64 | A measure of atomic displacement (temperature factor), indicating the flexibility of atoms in the structure. |
| R Free | float64 | A cross-validation metric that assesses the quality of the crystallographic model against experimental data. |
| R Work | float64 | A measure of how well the model fits the experimental X-ray diffraction data during refinement. |
| Structure Title | string | The name or title assigned to the protein structure by the researchers. |
| Sequence | string | The linear sequence of amino acids in the protein. |
| Entity Polymer Type | string | The type of polymer present (typically a polypeptide or protein). |
| Polymer Entity Sequence Length | float64 | The length (number of residues) of the polymer or protein sequence. |
| Entity Macromolecule Type | string | The classification of the macromolecule (e.g., protein, nucleic acid). |
| Total Number of polymer Entity Instances (Chains) per Entity | float64 | The number of chains for each polymer entity. |
| Molecular Weight (Entity) | float64 | The molecular weight of each individual polymer entity (e.g., a protein or nucleic acid). |
| Macromolecule Name | string | The name of the macromolecule or protein. |
| EC Number | string | The Enzyme Commission (EC) number, a numerical classification for enzymes based on their function. |
| EC Provenance Source | string | The source of the enzyme classification information. |
| Source Organism | string | The organism from which the protein or macromolecule was derived (e.g., Homo sapiens). |
| Taxonomy ID | float64 | The taxonomy identifier that links to the classification of the source organism. |
| Total Number of Polymer Residues per Assembly | float64 | The total number of residues in the entire protein assembly (multiple chains combined). |
| Total Number of Polymer Instances (Chains) per Assembly | float64 | The total number of polymer chains in the entire assembly. |
| Oligomeric Count | float64 | The number of subunits in the protein's oligomeric state (e.g., monomer, dimer, trimer). |
| Assembly ID | float64 | A unique identifier for the specific assembly in the PDB. |
| Oligomeric State | string | The oligomeric form of the protein (e.g., monomer, dimer, tetramer), indicating how many subunits are involved in forming the functional unit. |
| Stoichiometry | string | The specific ratio of components (subunits or molecules) in a protein assembly. |
| Ligand ID | string | A unique identifier for any ligand (small molecule) bound to the protein in the structure. |
| Ligand Formula | string | The chemical formula of the ligand. |
| Ligand MW | float64 | The molecular weight of the bound ligand. |
| Ligand Name | string | The name of the ligand. |
| InChI | string | The International Chemical Identifier for the ligand, providing a textual representation of its chemical structure. |
| Ligand SMILES | string | A string representation of the ligand’s structure using the SMILES notation. |
| Ligand of Interest | string | Specifies whether a particular ligand is of special interest in the structure (e.g., a drug or cofactor). |
| index_level_0 | int64 | auto-generated, Not biologically meaningful. |
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