Structure of PDB 4v81 Chain f

Receptor sequence
>4v81f (length=533) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MSLQLLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGA
GNIKLTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGE
LLRQAHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFL
LQVARSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQ
HLSPKDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSG
FFYSSADQRDKLAASERKFVDAKLKKIIDLKFVIINQKGIDPMSLDVFAK
HNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFSGLVYQETIGE
EKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRAVANVLKDKNI
IPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEALLVIPKTLVKN
SGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDPTIEGIWDSYR
VLRNAITGATGIASNLLLCDELLRAGRSTLKET
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Chainf
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 f L1037 P1039 K1057 D1089 T1092 T1093 A1415 Y1419 V1491 L37 P39 K57 D89 T92 T93 A404 Y408 V480
BS02 BEF f K1057 D1089 K57 D89
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
UniProtP39079|TCPZ_YEAST T-complex protein 1 subunit zeta (Gene Name=CCT6)

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