Structure of PDB 7yly Chain z

Receptor sequence
>7ylyz (length=538) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
SLQLLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGAG
NIKLTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGEL
LRQAHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFLL
QVARSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQH
LSPKDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSGF
FYSSADQRDKLAASERKFVDAKLKKIIDLKNEVCGMDPDKGFVIINQKGI
DPMSLDVFAKHNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFS
GLVYQETIGEEKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRA
VANVLKDKNIIPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEAL
LVIPKTLVKNSGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDP
TIEGIWDSYRVLRNAITGATGIASNLLLCDELLRAGRS
3D structure
PDB7yly Structural basis of plp2-mediated cytoskeletal protein folding by TRiC/CCT.
Chainz
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 z L37 D89 G90 T160 A415 D508 L36 D88 G89 T159 A414 D507
BS02 AF3 z D58 D89 K161 D397 D57 D88 K160 D396
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
GO:0051086 chaperone mediated protein folding independent of cofactor
Cellular Component
GO:0005737 cytoplasm
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:7yly, PDBe:7yly, PDBj:7yly
PDBsum7yly
PubMed36921056
UniProtP39079|TCPZ_YEAST T-complex protein 1 subunit zeta (Gene Name=CCT6)

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