Structure of PDB 6ks6 Chain h

Receptor sequence

>6ks6h (length=527) Species: 559292 (Saccharomyces cerevisiae S288C)

MNFGSQTPTIVVLKEGTDASQGKGQIISNINACVAVQEALKPTLGPLGSD
ILIVTSNQKTTISNDGATILKLLDVVHPAAKTLVDISRAQDAEVGDGTTS
VTILAGELMKEAKPFLEEGISSHLIMKGYRKAVSLAVEKINELAVDITSE
KSSGRELLERCARTAMSSKLIHNNADFFVKMCVDAVLSLDRNDLDDKLIG
IKKIPGGAMEESLFINGVAFKKTFSYAGFEQQPKKFNNPKILSLNVELEL
KAEKDNAEVRVEHVEDYQAIVDAEWQLIFEKLRQVEETGANIVLSKLPIG
DLATQFFADRNIFCAGRVSADDMNRVIQAVGGSIQSTTSDIKPEHLGTCA
LFEEMQIGSERYNLFQGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIV
KRALQNKLIVAGGGATEMEVSKCLRDYSKTIAGKQQMIINAFAKALEVIP
RQLCENAGFDAIEILNKLRLAHSKGEKWYGVVFETENIGDNFAKFVWEPA
LVKINALNSATEATNLILSVDETITNK

3D structure

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

Enzymatic activity

• Catalytic site (original residue number in PDB): D65 T98 T99 D395
• Catalytic site (residue number reindexed from 1): D65 T98 T99 D395

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	h	L44 G45 P46 D96 G97 S167 S168 G413 E498	L44 G45 P46 D96 G97 S167 S168 G413 E498
BS02	AF3	h	D65 T98 T99 D395	D65 T98 T99 D395

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: P42943|TCPH_YEAST T-complex protein 1 subunit eta (Gene Name=CCT7)