Structure of PDB 7yly Chain E

Receptor sequence
>7ylyE (length=536) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
EMGRPFIIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKI
LISPDGEITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVV
VLASALLDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASND
ELFRDFLLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDL
IKMQGRVGGSISDSKLINGVILDKDFSHPQMPKCVLPKEGSDGVKLAILT
CPFEPPKPKTKHKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVIC
QWGFDDEANHLLLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDK
LGTCSRIYEQEFGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERAL
HDSLCVVRNLVKDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFA
QALDTIPMTLAENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMK
ELFVVDPFIGKKQQILLATQLCRMILKIDNVIISGK
3D structure
PDB7yly Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
ChainE
Resolution3.05 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 L65 G118 T120 S190 G443 L42 G95 T97 S167 G420
BS02 AF3 E D86 K191 D425 D63 K168 D402
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:7yly, PDBe:7yly, PDBj:7yly
PDBsum7yly
PubMed36921056
UniProtP40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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