Structure of PDB 4v8r Chain Az

Receptor sequence
>4v8rAz (length=531) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
LLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGAGNIK
LTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGELLRQ
AHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFLLQVA
RSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQHLSP
KDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSGFFYS
SADQRDKLAASERKFVDAKLKKIIDLKNEVCGMDPFVIINQKGIDPMSLD
VFAKHNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFSGLVYQE
TIGEEKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRAVANVLK
DKNIIPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEALLVIPKT
LVKNSGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDPTIEGIW
DSYRVLRNAITGATGIASNLLLCDELLRAGR
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainAz
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 Az L1037 G1038 P1039 G1090 T1092 T1093 T1160 A1415 D1508 L33 G34 P35 G86 T88 T89 T156 A408 D501
BS02 BEF Az D1058 T1091 T1092 K1161 D54 T87 T88 K157
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:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP39079|TCPZ_YEAST T-complex protein 1 subunit zeta (Gene Name=CCT6)

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