Structure of PDB 4v8r Chain Bh

Receptor sequence

>4v8rBh (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: Bh
• 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	Bh	L4044 G4045 G4097 T4098 T4099 S4100 T4164 S4168 G4413 L4453 E4498	L35 G36 G88 T89 T90 S91 T155 S159 G404 L444 E489
BS02	BEF	Bh	N4064 D4096 T4098 T4099 K4169 D4395	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)