Structure of PDB 6ks6 Chain z

Receptor sequence
>6ks6z (length=538) Species: 559292 (Saccharomyces cerevisiae S288C) [Search protein sequence]
SLQLLNPKAESLRRDAALKVNVTSAEGLQSVLETNLGPKGTLKMLVDGAG
NIKLTKDGKVLLTEMQIQSPTAVLIARAAAAQDEITGDGTTTVVCLVGEL
LRQAHRFIQEGVHPRIITDGFEIARKESMKFLDEFKISKTNLSNDREFLL
QVARSSLLTKVDADLTEVLTPIVTDAVLSVYDAQADNLDLHMVEIMQMQH
LSPKDTTFIKGLVLDHGGRHPDMPTRVKNAYVLILNVSLEYEKTEVNSGF
FYSSADQRDKLAASERKFVDAKLKKIIDLKNEVCGMDPDKGFVIINQKGI
DPMSLDVFAKHNILALRRAKRRNMERLQLVTGGEAQNSVEDLSPQILGFS
GLVYQETIGEEKFTYVTENTDPKSCTILIKGSTHYALAQTKDAVRDGLRA
VANVLKDKNIIPGAGAFYIALSRYLRSANMNKLGAKGKTKTGIEAFAEAL
LVIPKTLVKNSGFDPLDVLAMVEDELDDAQDSDETRYVGVDLNIGDSCDP
TIEGIWDSYRVLRNAITGATGIASNLLLCDELLRAGRS
3D structure
PDB6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
Chainz
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) D58 T91 T92 D397
Catalytic site (residue number reindexed from 1) D57 T90 T91 D396
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 P39 D89 G90 T160 A415 I506 D508 L36 P38 D88 G89 T159 A414 I505 D507
BS02 AF3 z D58 D89 T91 T92 K161 D57 D88 T90 T91 K160
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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Biological Process
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Cellular Component
External links
PDB RCSB:6ks6, PDBe:6ks6, PDBj:6ks6
PDBsum6ks6
PubMed31492816
UniProtP39079|TCPZ_YEAST T-complex protein 1 subunit zeta (Gene Name=CCT6)

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