Structure of PDB 1q2v Chain D

Receptor sequence
>1q2vD (length=518) [Search protein sequence]
VVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGD
IVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELL
RKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIA
ATSITGKNAESHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGE
GVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKIN
ITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKY
GIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGE
NMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVL
PAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLD
TVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSA
SEAAIMILRIDDVIAAKA
3D structure
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.
ChainD
Resolution2.4 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SO4 D G96 T98 T99 G88 T90 T91
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1q2v, PDBe:1q2v, PDBj:1q2v
PDBsum1q2v
PubMed14729342
UniProtP61112|THSA_THEK1 Thermosome subunit alpha (Gene Name=thsA)

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