Structure of PDB 4v8r Chain AE

Receptor sequence
>4v8rAE (length=528) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
KDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKILISPDGEIT
ITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVVLASALLDQ
ALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDELFRDFLLR
AAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLIKMQGRVGG
SISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILTCPFEPPKPK
TKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQWGFDDEAN
HLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKLGTCSRIYE
QEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALHDSLCVVRN
LVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQALDTIPMT
LAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKELFVVDPFI
GKKQQILLATQLCRMILKIDNVIISGKD
3D structure
PDB4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
ChainAE
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 AE L65 P67 D117 G118 T120 S190 G443 C514 V527 D529 L33 P35 D85 G86 T88 S158 G411 C482 V495 D497
BS02 BEF AE N85 D86 D117 T119 T120 K191 N53 D54 D85 T87 T88 K159
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:4v8r, PDBe:4v8r, PDBj:4v8r
PDBsum4v8r
PubMed23478063
UniProtP40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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