Structure of PDB 4v94 Chain k

Receptor sequence
>4v94k (length=513) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
VFMNASQERTTGRQAQISNITAAKAVADVIRTCLGPKAMLKMLLDPMGGL
VLTNDGHAILREIDVAHPAAKSMLELSRTQDEEVGDGTTTVIILAGEILA
QCAPYLIEKNIHPVIIIQALKKALTDALEVIKQVSKPVDVENDAAMKKLI
QASIGTKYVIHWSEKMCELALDAVKTVREIDIKRYVRVEKIPGGDVLDSR
VLKGVLLNKDVVHPKMSRHIENPRVVLLDCPLEYKKGESQTNIEIEKEED
WNRILQIEEEQVQLMCEQILAVRPTLVITEKGVSDLAQHYLLKGGCSVLR
RVKKSDNNRIARVTGATIVNRVEDLKESDVGTNCGLFKVEMIGDEYFSFL
DNGSGKACTIMLRGGSKDILNEIDRNLQDAMAVARNVMLSPSLSPGGGAT
EMAVSVKLAEKAKQLEGIQQWPYQAVADAMECIPRTLIQNAGGDPIRLLS
QLRAKHAQGNFTTGIDGDKGKIVDMVSYGIWEPEVIKQQSVKTAIESACL
LLRVDDIVSGVRK
3D structure
PDB4v94 The Molecular Architecture of the Eukaryotic Chaperonin TRiC/CCT.
Chaink
Resolution3.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D398
Catalytic site (residue number reindexed from 1) D379
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 k L39 G40 D91 G92 T94 T95 T161 G416 G486 I499 E501 L34 G35 D86 G87 T89 T90 T156 G397 G467 I480 E482
BS02 BEF k N59 D60 G61 D91 T93 T94 N54 D55 G56 D86 T88 T89
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

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Molecular Function
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Biological Process
External links
PDB RCSB:4v94, PDBe:4v94, PDBj:4v94
PDBsum4v94
PubMed22503819
UniProtP39077|TCPG_YEAST T-complex protein 1 subunit gamma (Gene Name=CCT3)

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