Structure of PDB 6ks6 Chain d

Receptor sequence

>6ks6d (length=524) Species: 559292 (Saccharomyces cerevisiae S288C)

VPSNATFKNKEKPQEVRKANIIAARSVADAIRTSLGPKGMDKMIKTSRGE
IIISNDGHTILKQMAILHPVARMLVEVSAAQDSEAGDGTTSVVILTGALL
GAAERLLNKGIHPTIIADSFQSAAKRSVDILLEMCHKVSLSDREQLVRAA
STSLSSKIVSQYSSFLAPLAVDSVLKISDENSKNVDLNDIRLVKKVGGTI
DDTEMIDGVVLTQTAIKSAGGPTRKEKAKIGLIQFQISPPKPDTENNIIV
NDYRQMDKILKEERAYLLNICKKIKKAKCNVLLIQKSILRDAVNDLALHF
LSKLNIMVVKDIEREEIEFLSKGLGCKPIADIELFTEDRLGSADLVEEID
SDGSKIVRVTGIRNNNARPTVSVVIRGANNMIIDETERSLHDALCVIRCL
VKERGLIAGGGAPEIEISRRLSKEARSMEGVQAFIWQEFASALEVIPTTL
AENAGLNSIKVVTELRSKHENGELNDGISVRRSGTTNTYEEHILQPVLVS
TSAITLASECVKSILRIDDIAFSR

3D structure

• PDB: 6ks6 An ensemble of cryo-EM structures of TRiC reveal its conformational landscape and subunit specificity.
• Chain: d
• Resolution: 2.99 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D60 T93 T94 D396
• Catalytic site (residue number reindexed from 1): D56 T89 T90 D392

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	d	G40 P41 D91 G92 T94 T156 S159 G414 V484 I497 Q499	G36 P37 D87 G88 T90 T152 S155 G410 V480 I493 Q495
BS02	MG	d	D91 S157	D87 S153
BS03	AF3	d	D60 T93 T94 K161 D396	D56 T89 T90 K157 D392

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

External links

• PDB: RCSB:6ks6, PDBe:6ks6, PDBj:6ks6
• PDBsum: 6ks6
• PubMed: 31492816
• UniProt: P39078|TCPD_YEAST T-complex protein 1 subunit delta (Gene Name=CCT4)