› 3qfp

X-ray diffraction
2.26Å resolution

Crystal structure of yeast Hsp70 (Bip/Kar2) ATPase domain

Released:
DOI: 10.2210/pdb3qfp/pdb
PDB entry 3qfp coloured by chain, front view.
PDB entry 3qfp coloured by chain, side view.
PDB entry 3qfp coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor.
Yan M, Li J, Sha B
Biochem J 438 447-55 (2011)
PMID: 21675960

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147743 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum chaperone BiP Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 42.45 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P16474 (Residues: 43-426; Coverage: 60%)
Gene names: GRP78, J1248, KAR2, SSD1, YJL034W
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand PO4 1 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 64.004Å b: 64.053Å c: 100.401Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.237 0.235 0.265
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Molecular chaperone functions in protein folding and proteostasis.
Kim et al. (2013)
12 more

3 mentions without citation

The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite.
Day et al. (2019)
2 more