Structure of PDB 1q3s Chain D Binding Site BS01

Receptor Information
>1q3s Chain D (length=517) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDI
VVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELLR
KAEELLDQNIHPSIIIKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAA
TSITGKNAESHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGEG
VEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKINI
TSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYG
IMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGEN
MIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLP
AGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDT
VEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSAS
EAAIMILRIDDVIAAKA
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain1q3s Chain D Residue 4528 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB1q3s Crystal Structures of the Group II Chaperonin from Thermococcus strain KS-1: Steric Hindrance by the Substituted Amino Acid, and Inter-subunit Rearrangement between Two Crystal Forms.
Resolution3.0 Å
Binding residue
(original residue number in PDB)		G44 P45 D95 G96 T97 T98 T99 G164 A410 G411 L451 I479 D480 V481 F482 E496
Binding residue
(residue number reindexed from 1)		G35 P36 D86 G87 T88 T89 T90 G155 A401 G402 L442 I470 D471 V472 F473 E487
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) D64 T97 T98 D393
Catalytic site (residue number reindexed from 1) D55 T88 T89 D384
Enzyme Commision number 3.6.4.9: Transferred entry: 5.6.1.7.
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0016887 ATP hydrolysis activity
GO:0051082 unfolded protein binding
GO:0140662 ATP-dependent protein folding chaperone
Biological Process
GO:0006457 protein folding

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:1q3s, PDBe:1q3s, PDBj:1q3s
PDBsum1q3s
PubMed14729342
UniProtP61112|THSA_THEK1 Thermosome subunit alpha (Gene Name=thsA)

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