Structure of PDB 1q3q Chain D

Receptor sequence
>1q3qD (length=518) [Search protein sequence]
VVILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGD
IVVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELL
RKAEELLDQNIHPSIITKGYALAAEKAQEILDEIAIRVDPDDEETLLKIA
ATSITGKNAESHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGE
GVEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKIN
ITSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKY
GIMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGE
NMIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVL
PAGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLD
TVEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSA
SEAAIMILRIDDVIAAKA
3D structure
PDB1q3q 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
Resolution2.3 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 MG D D95 K165 D87 K157
BS02 ANP D L43 G44 P45 D95 G96 T97 T98 T99 A410 G411 L451 I494 E496 L35 G36 P37 D87 G88 T89 T90 T91 A402 G403 L443 I486 E488
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:1q3q, PDBe:1q3q, PDBj:1q3q
PDBsum1q3q
PubMed14729342
UniProtP61112|THSA_THEK1 Thermosome subunit alpha (Gene Name=thsA)

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