Structure of PDB 4v81 Chain D

Receptor sequence
>4v81D (length=522) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SNATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGEII
ISNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALLGA
AERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAAST
SLSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTIDD
TEMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIVND
YRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHFLS
KLNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLDSADLVEEIDSD
GSKIVRVTGIRNNNARPTVSVVIRGANNMIIDETERSLHDALCVIRCLVK
ERGLIAGGGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTLAE
NAGLNSIKVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVSTS
AITLASECVKSILRIDDIAFSR
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
ChainD
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) D60 T93 T94 D396
Catalytic site (residue number reindexed from 1) D54 T87 T88 D390
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 D G40 P41 D91 L454 R485 Q499 G34 P35 D85 L448 R479 Q493
BS02 BEF D D91 G92 T93 T94 S95 D85 G86 T87 T88 S89
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:4v81, PDBe:4v81, PDBj:4v81
PDBsum4v81
PubMed21701561
UniProtP39078|TCPD_YEAST T-complex protein 1 subunit delta (Gene Name=CCT4)

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