Structure of PDB 4v94 Chain P

Receptor sequence
>4v94P (length=521) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
PQNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGRNKII
VNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVMI
LAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKND
KNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPYFNVDSIRVVKIMG
GSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFTCPLDIANTETKGT
VLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYLN
RYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEIG
GDRVTVFKQRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMKPSGGKLL
PGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTLAETAGLD
VNEVLPNLYAAHNTDHLYKGVDIDGESDEGVKDIREENIYDMLATKKFAI
NVATEAATTVLSIDQIIMAKK
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
ChainP
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) D67 T100 N101
Catalytic site (residue number reindexed from 1) D62 T95 N96
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 P M46 G47 P48 D98 G99 T100 N101 S169 G422 A423 D519 M41 G42 P43 D93 G94 T95 N96 S164 G402 A403 D491
BS02 BEF P D98 T100 N101 K170 D403 D93 T95 N96 K165 D383
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP47079|TCPQ_YEAST T-complex protein 1 subunit theta (Gene Name=CCT8)

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