Structure of PDB 4v8r Chain Ah

Receptor sequence

>4v8rAh (length=519) Species: 4932 (Saccharomyces cerevisiae)

IVVLKEGTDASQGKGQIISNINACVAVQEALKPTLGPLGSDILIVTSNQK
TTISNDGATILKLLDVVHPAAKTLVDISRAQDAEVGDGTTSVTILAGELM
KEAKPFLEEGISSHLIMKGYRKAVSLAVEKINELAVDITSEKSSGRELLE
RCARTAMSSKLIHNNADFFVKMCVDAVLSLDRNDLDDKLIGIKKIPGGAM
EESLFINGVAFKKTFSYAGFEQQPKKFNNPKILSLNVELELKAEKDNAEV
RVEHVEDYQAIVDAEWQLIFEKLRQVEETGANIVLSKLPIGDLATQFFAD
RNIFCAGRVSADDMNRVIQAVGGSIQSTTSDIKPEHLGTCALFEEMQIGS
ERYNLFQGCPQAKTCTLLLRGGAEQVIAEVERSLHDAIMIVKRALQNKLI
VAGGGATEMEVSKCLRDYSKTIAGKQQMIINAFAKALEVIPRQLCENAGF
DAIEILNKLRLAHSKGEKWYGVVFETENIGDNFAKFVWEPALVKINALNS
ATEATNLILSVDETITNKG

3D structure

• PDB: 4v8r The Crystal Structures of the Eukaryotic Chaperonin Cct Reveal its Functional Partitioning
• Chain: Ah
• Resolution: 3.8 Å

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	Ah	L1044 G1045 G1097 T1098 T1099 S1100 T1164 S1168 G1413 L1453 E1498	L35 G36 G88 T89 T90 S91 T155 S159 G404 L444 E489
BS02	BEF	Ah	N1064 D1096 T1098 T1099 K1169 D1395	N55 D87 T89 T90 K160 D386

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:4v8r, PDBe:4v8r, PDBj:4v8r
• PDBsum: 4v8r
• PubMed: 23478063
• UniProt: P42943|TCPH_YEAST T-complex protein 1 subunit eta (Gene Name=CCT7)