Structure of PDB 1q3s Chain F

Receptor sequence
>1q3sF (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.
ChainF
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 F G44 P45 D95 G96 T97 T98 T99 G164 A410 G411 L451 V481 F482 E496 G35 P36 D86 G87 T88 T89 T90 G155 A401 G402 L442 V472 F473 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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