Structure of PDB 4v81 Chain b

Receptor sequence
>4v81b (length=513) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
VQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSN
TCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAEL
LREAEKLIDIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFREDLIH
IAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGKLSD
SFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKVDST
AKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLGINS
IEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQPFLK
FSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVLGGG
CAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDSSEL
VSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSASEAA
EVLLRVDNIIRAR
3D structure
PDB4v81 The crystal structure of yeast CCT reveals intrinsic asymmetry of eukaryotic cytosolic chaperonins.
Chainb
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 b L1037 G1038 D1090 G1091 T1093 G1404 L1444 I1487 E1489 L35 G36 D88 G89 T91 G399 L439 I482 E484
BS02 BEF b D1059 D1090 G1091 T1092 T1093 D1386 D57 D88 G89 T90 T91 D381
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:0005829 cytosol
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
UniProtP39076|TCPB_YEAST T-complex protein 1 subunit beta (Gene Name=CCT2)

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