Structure of PDB 4v94 Chain m

Receptor sequence
>4v94m (length=535) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
MGRPFIIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKIL
ISPDGEITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVV
LASALLDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDE
LFRDFLLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLI
KMQGRVGGSISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILTC
PFEPPKPKTKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQ
WGFDDEANHLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKL
GTCSRIYEQEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALH
DSLCVVRNLVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQ
ALDTIPMTLAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKE
LFVVDPFIGKKQQILLATQLCRMILKIDNVIISGK
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
Chainm
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 MG m D117 S187 D93 S163
BS02 ADP m L65 G66 G118 T120 G121 S190 G443 V527 L41 G42 G94 T96 G97 S166 G419 V503
BS03 BEF m N85 D117 T119 T120 K191 D425 N61 D93 T95 T96 K167 D401
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:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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