Structure of PDB 7yly Chain a

Receptor sequence
>7ylya (length=546) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
QLFNNSRSDTLFLGGEKISGDDIRNQNVLATMAVANVVKSSLGPVGLDKM
LVDDIGDFTVTNDGATILSLLDVQHPAGKILVELAQQQDREIGDGTTSVV
IIASELLKRANELVKNKIHPTTIITGFRVALREAIRFINEVLSTSVDTLG
KETLINIAKTSMSSKIIGADSDFFSNMVVDALLAVKTQNSKGEIKYPVKA
VNVLKAHGKSATESLLVPGYALNCTVASQAMPKRIAGGNVKIACLDLNLQ
KARMAMGVQINIDDPEQLEQIRKREAGIVLERVKKIIDAGAQVVLTTKGI
DDLCLKEFVEAKIMGVRRCKKEDLRRIARATGATLVSSMSNLEGEETFES
SYLGLCDEVVQAKFSDDECILIKGTSKHSSSSIILRGANDYSLDEMERSL
HDSLSVVKRTLESGNVVPGGGCVEAALNIYLDNFATTVGSREQLAIAEFA
AALLIIPKTLAVNAAKDSSELVAKLRSYHAASQMAKPEKRRSYRNYGLDL
IRGKIVDEIHAGVLEPTISKVKSLKSALEACVAILRIDTMITVDPE
3D structure
PDB7yly Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Chaina
Resolution3.05 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 a P46 D65 S165 S166 K167 G421 G422 P44 D63 S163 S164 K165 G419 G420
BS02 AF3 a D65 D96 T98 D404 D63 D94 T96 D402
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:0005832 chaperonin-containing T-complex
GO:0005886 plasma membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:7yly, PDBe:7yly, PDBj:7yly
PDBsum7yly
PubMed36921056
UniProtP12612|TCPA_YEAST T-complex protein 1 subunit alpha (Gene Name=TCP1)

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