Structure of PDB 1q3s Chain B

Receptor sequence
>1q3sB (length=517) [Search protein sequence]
VILPEGTQRYVGRDAQRLNILAARIIAETVRTTLGPKGMDKMLVDSLGDI
VVTNDCATILDKIDLQHPAAKMMVEVAKTQDKEAGDGTTTAVVIAGELLR
KAEELLDQNIHPSIIIKGYALAAEKAQEILDEIAIRVDPDDEETLLKIAA
TSITGKNAESHKELLAKLAVEAVKQVAEKKDGKYVVDLDNIKFEKKAGEG
VEESELVRGVVIDKEVVHPRMPKRVENAKIALINEALEVKKTETDAKINI
TSPDQLMSFLEQEEKMLKDMVDHIAQTGANVVFVQKGIDDLAQHYLAKYG
IMAVRRVKKSDMEKLAKATGAKIVTNVKDLTPEDLGYAEVVEERKLAGEN
MIFVEGCKNPKAVTILIRGGTEHVIDEVERALEDAVKVVKDVMEDGAVLP
AGGAPEIELAIRLDEYAKQVGGKEALAIENFADALKIIPKTLAENAGLDT
VEMLVKVISEHKNRGLGIGIDVFEGKPADMLEKGIIEPLRVKKQAIKSAS
EAAIMILRIDDVIAAKA
3D structure
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.
ChainB
Resolution3.0 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) D55 T88 T89 D384
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 ADP B G44 P45 G96 T97 T98 T99 G164 G411 L451 I479 V481 E496 G35 P36 G87 T88 T89 T90 G155 G402 L442 I470 V472 E487
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:1q3s, PDBe:1q3s, PDBj:1q3s
PDBsum1q3s
PubMed14729342
UniProtP61112|THSA_THEK1 Thermosome subunit alpha (Gene Name=thsA)

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