Structure of PDB 4v81 Chain G

Receptor sequence
>4v81G (length=509) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GTDASQGKGQIISNINACVAVQEALKPTLGPLGSDILIVTSNQKTTISND
GATILKLLDVVHPAAKTLVDISRAQDAEVGDGTTSVTILAGELMKEAKPF
LEEGISSHLIMKGYRKAVSLAVEKINELAVDITSELLERCARTAMSSKLI
HNNADFFVKMCVDAVLSLDRNDLDDKLIGIKKIPGGAMEESLFINGVAFK
KTFSYAGFEQQPKKFNNPKILSLNVELELKAEKDNAEVRVEHVEDYQAIV
DAEWQLIFEKLRQVEETGANIVLSKLPIGDLATQFFADRNIFCAGRVSAD
DMNRVIQAVGGSIQSTTSDIKPEHLGTCALFEEMQIGSERYNLFQGCPQA
KTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLIVAGGGATEMEVS
KCLRDYSKTIAGKQQMIINAFAKALEVIPRQLCENAGFDAIEILNKLRLA
HSKGEKWYGVVFETENIGDNFAKFVWEPALVKINALNSATEATNLILSVD
ETITNKGSE
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
ChainG
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) D50 T83 T84 D374
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 G T43 G45 D96 G97 T99 S100 S168 G413 L453 F483 E498 T28 G30 D81 G82 T84 S85 S147 G392 L432 F462 E477
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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Cellular Component
External links
PDB RCSB:4v81, PDBe:4v81, PDBj:4v81
PDBsum4v81
PubMed21701561
UniProtP42943|TCPH_YEAST T-complex protein 1 subunit eta (Gene Name=CCT7)

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