Structure of PDB 1q2v Chain D Binding Site BS01

Receptor Information
>1q2v Chain D (length=518) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGD
IVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELL
RKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIA
ATSITGKNAESHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGE
GVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKIN
ITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKY
GIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGE
NMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVL
PAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLD
TVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSA
SEAAIMILRIDDVIAAKA
Ligand information
Ligand IDSO4
InChIInChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
InChIKeyQAOWNCQODCNURD-UHFFFAOYSA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0[O-]S(=O)(=O)[O-]
CACTVS 3.341[O-][S]([O-])(=O)=O
ACDLabs 10.04[O-]S([O-])(=O)=O
FormulaO4 S
NameSULFATE ION
ChEMBL
DrugBankDB14546
ZINC
PDB chain1q2v Chain D Residue 4527 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1q2v 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.
Resolution2.4 Å
Binding residue
(original residue number in PDB)		G96 T98 T99
Binding residue
(residue number reindexed from 1)		G88 T90 T91
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D64 T97 T98 D393
Catalytic site (residue number reindexed from 1) D56 T89 T90 D385
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:1q2v, PDBe:1q2v, PDBj:1q2v
PDBsum1q2v
PubMed14729342
UniProtP61112|THSA_THEK1 Thermosome subunit alpha (Gene Name=thsA)

[Back to BioLiP]