Structure of PDB 6ks6 Chain g

Receptor sequence
>6ks6g (length=520) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
VVFMNASQERTTGRQAQISNITAAKAVADVIRTCLGPKAMLKMLLDPMGG
LVLTNDGHAILREIDVAHPAAKSMLELSRTQDEEVGDGTTTVIILAGEIL
AQCAPYLIEKNIHPVIIIQALKKALTDALEVIKQVSKPVDVENDAAMKKL
IQASIGTKYVIHWSEKMCELALDAVKTVRKDLNFEIDIKRYVRVEKIPGG
DVLDSRVLKGVLLNKDVVHPKMSRHIENPRVVLLDCPLEYKKGESQTNIE
IEKEEDWNRILQIEEEQVQLMCEQILAVRPTLVITEKGVSDLAQHYLLKG
GCSVLRRVKKSDNNRIARVTGATIVNRVEDLKESDVGTNCGLFKVEMIGD
EYFSFLDNCGLQKACTIMLRGGSKDILNEIDRNLQDAMAVARNVMLSPSL
SPGGGATEMAVSVKLAEKAKQLEGIQQWPYQAVADAMECIPRTLIQNAGG
DPIRLLSQLRAKHAQGNFTTGIDGDKGKIVDMVSYGIWEPEVIKQQSVKT
AIESACLLLRVDDIVSGVRK
3D structure
PDB6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Chaing
Resolution2.99 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D60 T93 T94 D458
Catalytic site (residue number reindexed from 1) D56 T89 T90 D386
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 g L39 P41 G92 T94 T95 T161 G476 G546 I559 E561 L35 P37 G88 T90 T91 T157 G404 G474 I487 E489
BS02 AF3 g D60 T93 T94 D56 T89 T90
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:6ks6, PDBe:6ks6, PDBj:6ks6
PDBsum6ks6
PubMed31492816
UniProtP39077|TCPG_YEAST T-complex protein 1 subunit gamma (Gene Name=CCT3)

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