Structure of PDB 4v94 Chain j

Receptor sequence
>4v94j (length=518) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
VQIFGDQVTEERAENARLSAFVGAIAVGDLVKSTLGPKGMDKLLQSASSN
TCMVTNDGATILKSIPLDNPAAKVLVNISKVQDDEVGDGTTSVTVLSAEL
LREAEKLIDQSKIHPQTIIEGYRLASAAALDALTKAAVDNSHDKTMFRED
LIHIAKTTLSSKILSQDKDHFAELATNAILRLKGSTNLEHIQIIKILGGK
LSDSFLDEGFILAKKFGNNQPKRIENAKILIANTTLDTDKVKIFGTKFKV
DSTAKLAQLEKAEREKMKNKIAKISKFGINTFINRQLIYDYPEQLFTDLG
INSIEHADFEGVERLALVTGGEVVSTFDEPSKCKLGECDVIEEIMLGEQP
FLKFSGCKAGEACTIVLRGATDQTLDEAERSLHDALSVLSQTTKETRTVL
GGGCAEMVMSKAVDTEAQNIDGKKSLAVEAFARALRQLPTILADNAGFDS
SELVSKLRSSIYNGISTSGLDLNNGTIADMRQLGIVESYKLKRAVVSSAS
EAAEVLLRVDNIIRARPR
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
Chainj
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 j T36 L37 G38 P39 G91 T93 S94 T159 S162 G403 G404 L444 I487 E489 T34 L35 G36 P37 G89 T91 S92 T157 S160 G401 G402 L442 I485 E487
BS02 BEF j D59 D90 T92 K164 D57 D88 T90 K162
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:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP39076|TCPB_YEAST T-complex protein 1 subunit beta (Gene Name=CCT2)

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