Structure of PDB 4v94 Chain E

Receptor sequence

>4v94E (length=535) Species: 559292 (Saccharomyces cerevisiae S288C)

MGRPFIIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKIL
ISPDGEITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVV
LASALLDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDE
LFRDFLLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLI
KMQGRVGGSISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILTC
PFEPPKPKTKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQ
WGFDDEANHLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKL
GTCSRIYEQEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALH
DSLCVVRNLVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQ
ALDTIPMTLAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKE
LFVVDPFIGKKQQILLATQLCRMILKIDNVIISGK

3D structure

• PDB: 4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
• Chain: E
• Resolution: 3.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D86 T119 T120 D425
• Catalytic site (residue number reindexed from 1): D62 T95 T96 D401

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	E	D117 S187	D93 S163
BS02	ADP	E	G66 P67 G118 T120 S190 G443 V527	G42 P43 G94 T96 S166 G419 V503
BS03	BEF	E	N85 D117 T119 T120 K191	N61 D93 T95 T96 K167

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

External links

• PDB: RCSB:4v94, PDBe:4v94, PDBj:4v94
• PDBsum: 4v94
• PubMed: 22503819
• UniProt: P40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)