Structure of PDB 7ylw Chain e

Receptor sequence
>7ylwe (length=535) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
MGRPFIIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKIL
ISPDGEITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVV
LASALLDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDE
LFRDFLLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLI
KMQGRVGGSISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILTC
PFEPPKPKTKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQ
WGFDDEANHLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKL
GTCSRIYEQEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALH
DSLCVVRNLVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQ
ALDTIPMTLAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKE
LFVVDPFIGKKQQILLATQLCRMILKIDNVIISGK
3D structure
PDB7ylw Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Chaine
Resolution3.39 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 e D117 G118 S190 G443 D93 G94 S166 G419
BS02 AF3 e D86 T119 K191 D425 D62 T95 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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7ylw, PDBe:7ylw, PDBj:7ylw
PDBsum7ylw
PubMed36921056
UniProtP40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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