Structure of PDB 4v81 Chain h

Receptor sequence
>4v81h (length=525) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LPQNPNAGLFKQGYNSYSNADGQIIKSIAAIRELHQMCLTSMGPCGRNKI
IVNHLGKIIITNDAATMLRELDIVHPAVKVLVMATEQQKIDMGDGTNLVM
ILAGELLNVSEKLISMGLSAVEIIQGYNMARKFTLKELDEMVVGEITDKN
DKNELLKMIKPVISSKKYGSEDILSELVSEAVSHVLPYFNVDSIRVVKIM
GGSLSNSTVIKGMVFNREPEGHVKSLSEDKKHKVAVFTCPLDIANTETKG
TVLLHNAQEMLDFSKGEEKQIDAMMKEIADMGVECIVAGAGVGELALHYL
NRYGILVLKVPSKFELRRLCRVCGATPLPRLGAPTPEELGLVETVKTMEI
GGDRVTVFKQEQGEISRTSTIILRGATQNNLDDIERAIDDGVAAVKGLMK
PSGGKLLPGAGATEIELISRITKYGERTPGLLQLAIKQFAVAFEVVPRTL
AETAGLDVNEVLPNLYAAHNVTEPGAVKTDHLYKGVDIDGESDEGVKDIR
EENIYDMLATKKFAINVATEAATTV
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Chainh
Resolution3.8 Å
3D
structure
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Enzymatic activity
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 h G1047 P1048 D1098 G1099 T1100 N1101 S1169 A1423 G43 P44 D94 G95 T96 N97 S165 A410
BS02 BEF h D1098 G1099 T1100 N1101 D94 G95 T96 N97
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:4v81, PDBe:4v81, PDBj:4v81
PDBsum4v81
PubMed21701561
UniProtP47079|TCPQ_YEAST T-complex protein 1 subunit theta (Gene Name=CCT8)

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