› 2qw9

X-ray diffraction
1.85Å resolution

Crystal structure of bovine hsc70 (1-394aa)in the apo state

Released:
DOI: 10.2210/pdb2qw9/pdb
PDB entry 2qw9 coloured by chain, front view.
PDB entry 2qw9 coloured by chain, side view.
PDB entry 2qw9 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis of J cochaperone binding and regulation of Hsp70.
Jiang J, Maes EG, Taylor AB, Wang L, Hinck AP, Lafer EM, Sousa R
Mol Cell 28 422-33 (2007)
PMID: 17996706

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock cognate 71 kDa protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 394 amino acids
Theoretical weight: 43.42 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P19120 (Residues: 1-394; Coverage: 61%)
Gene names: HSC70, HSPA8
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 73.336Å b: 78.236Å c: 75.462Å
α: 90° β: 100.81° γ: 90°
R-values:
R R work R free
0.204 0.202 0.236
Expression system: Escherichia coli

Quick links

Citations

34 review citations

The HSP70 chaperone machinery: J proteins as drivers of functional specificity.
Kampinga et al. (2010)
33 more

5 mentions without citation

Allostery in the Hsp70 chaperone proteins.
Zuiderweg et al. (2013)
4 more