› 3iuc

X-ray diffraction
2.4Å resolution

Crystal structure of the human 70kDa heat shock protein 5 (BiP/GRP78) ATPase domain in complex with ADP

Released:
DOI: 10.2210/pdb3iuc/pdb
PDB entry 3iuc coloured by chain, front view.
PDB entry 3iuc coloured by chain, side view.
PDB entry 3iuc coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.
Wisniewska M, Karlberg T, Lehtiö L, Johansson I, Kotenyova T, Moche M, Schüler H
PLoS One 5 e8625 (2010)
PMID: 20072699

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

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum chaperone BiP Chains: A, C
Molecule details ›
Chains: A, C
Length: 408 amino acids
Theoretical weight: 45.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P11021 (Residues: 26-410; Coverage: 61%)
Gene names: GRP78, HSPA5
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ADP 2 x ADP
Ligand CA 4 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P1
Unit cell:
a: 48.212Å b: 51.795Å c: 94.994Å
α: 98.85° β: 94.88° γ: 117.61°
R-values:
R R work R free
0.194 0.19 0.27
Expression system: Escherichia coli

Quick links

Citations

11 review citations

HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
Stricher et al. (2013)
10 more

13 mentions without citation

HSPA5 Gene encoding Hsp70 chaperone BiP in the endoplasmic reticulum.
Wang et al. (2017)
12 more