Structure of PDB 4v81 Chain e

Receptor sequence
>4v81e (length=525) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
IIVKDQGNKKRQHGLEAKKSHILAARSVASIIKTSLGPRGLDKILISPDG
EITITNDGATILSQMELDNEIAKLLVQLSKSQDDEIGDGTTGVVVLASAL
LDQALELIQKGIHPIKIANGFDEAAKLAISKLEETCDDISASNDELFRDF
LLRAAKTSLGSKIVSKDHDRFAEMAVEAVINVMDKDRKDVDFDLIKMQGR
VGGSISDSKLINGVILDKDFSHPQMPKEGSDGVKLAILTCPFEPPKPKTK
HKLDISSVEEYQKLQTYEQDKFKEMIDDVKKAGADVVICQWGFDDEANHL
LLQNDLPAVRWVGGQELEHIAISTNGRIVPRFQDLSKDKLGTCSRIYEQE
FGTTKDRMLIIEQSKETKTVTCFVRGSNKMIVDEAERALHDSLCVVRNLV
KDSRVVYGGGAAEVTMSLAVSEEADKQRGIDQYAFRGFAQALDTIPMTLA
ENSGLDPIGTLSTLKSKQLKEKISNIGVDCLGYGSNDMKELFVVDPFIGK
KQQILLATQLCRMILKIDNVIISGK
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Chaine
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 ADP e G1066 P1067 D1117 G1118 T1120 G1121 T1186 G1443 L1483 V1512 D1513 V1527 G37 P38 D88 G89 T91 G92 T157 G409 L449 V478 D479 V493
BS02 BEF e D1086 D1117 G1118 T1119 T1120 D1425 D57 D88 G89 T90 T91 D391
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:4v81, PDBe:4v81, PDBj:4v81
PDBsum4v81
PubMed21701561
UniProtP40413|TCPE_YEAST T-complex protein 1 subunit epsilon (Gene Name=CCT5)

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