Structure of PDB 4v94 Chain O

Receptor sequence
>4v94O (length=526) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
NFGSQTPTIVVLKEGTDASQGKGQIISNINACVAVQEALKPTLGPLGSDI
LIVTSNQKTTISNDGATILKLLDVVHPAAKTLVDISRAQDAEVGDGTTSV
TILAGELMKEAKPFLEEGISSHLIMKGYRKAVSLAVEKINELAVDITSEK
SSGRELLERCARTAMSSKLIHNNADFFVKMCVDAVLSLDRNDLDDKLIGI
KKIPGGAMEESLFINGVAFKKTFSYAGFEQQPKKFNNPKILSLNVELELK
AEKDNAEVRVEHVEDYQAIVDAEWQLIFEKLRQVEETGANIVLSKLPIGD
LATQFFADRNIFCAGRVSADDMNRVIQAVGGSIQSTTSDIKPEHLGTCAL
FEEMQIGSERYNLFQGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVK
RALQNKLIVAGGGATEMEVSKCLRDYSKTIAGKQQMIINAFAKALEVIPR
QLCENAGFDAIEILNKLRLAHSKGEKWYGVVFETENIGDNFAKFVWEPAL
VKINALNSATEATNLILSVDETITNK
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
ChainO
Resolution3.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D65 T98 T99 D395
Catalytic site (residue number reindexed from 1) D64 T97 T98 D394
Enzyme Commision number ?
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 O L44 G45 G97 T98 T99 S100 T164 S167 S168 G413 L43 G44 G96 T97 T98 S99 T163 S166 S167 G412
BS02 BEF O N64 D65 D96 T98 T99 K169 D395 N63 D64 D95 T97 T98 K168 D394
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
GO:0051086 chaperone mediated protein folding independent of cofactor
Cellular Component
GO:0005737 cytoplasm
GO:0005832 chaperonin-containing T-complex

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Biological Process
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Cellular Component
External links
PDB RCSB:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP42943|TCPH_YEAST T-complex protein 1 subunit eta (Gene Name=CCT7)

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