Structure of PDB 6ks6 Chain e

Receptor sequence
>6ks6e (length=535) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
MGRPFIIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKIL
ISPDGEITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVV
LASALLDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDE
LFRDFLLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLI
KMQGRVGGSISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILTC
PFEPPKPKTKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQ
WGFDDEANHLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKL
GTCSRIYEQEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALH
DSLCVVRNLVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQ
ALDTIPMTLAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKE
LFVVDPFIGKKQQILLATQLCRMILKIDNVIISGK
3D structure
PDB6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Chaine
Resolution2.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D86 T119 T120 D425
Catalytic site (residue number reindexed from 1) D62 T95 T96 D401
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 G66 P67 D117 G118 T186 S190 G442 G443 D529 K534 G42 P43 D93 G94 T162 S166 G418 G419 D505 K510
BS02 AF3 e D86 T119 T120 K191 D425 D62 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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6ks6, PDBe:6ks6, PDBj:6ks6
PDBsum6ks6
PubMed31492816
UniProtP40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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