› 2p32

X-ray diffraction
3.2Å resolution

Crystal structure of the C-terminal 10 kDa subdomain from C. elegans Hsp70

Released:
DOI: 10.2210/pdb2p32/pdb
PDB 2p32 coloured by chain and viewed from the front.
PDB 2p32 coloured by chain and viewed from the side.
PDB 2p32 coloured by chain and viewed from the top.
Source organism: Caenorhabditis elegans
Primary publication:
Crystal structure of the C-terminal three-helix bundle subdomain of C. elegans Hsp70.
Worrall LJ, Walkinshaw MD
Biochem. Biophys. Res. Commun. 357 105-10 (2007)
PMID: 17407764

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein hsp-1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 120 amino acids
Theoretical weight: 12.96 KDa
Source organism: Caenorhabditis elegans
Expression system: Escherichia coli
UniProt:
  • Canonical: P09446 (Residues: 542-640; Coverage: 16%)
Gene names: F26D10.3, hsp-1, hsp70a
Structure domains: Substrate Binding Domain Of Dnak; Chain:A; Domain 2

Ligands and Environments

1 bound ligand:
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P42212
Unit cell:
a: 138.927Å b: 138.927Å c: 100.704Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.269 0.268 0.282
Expression system: Escherichia coli

Quick links

Citations

9 citation in other articles

Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain.
Aprile et al. (2013)
8 more

5 mentions without citation

Identification of an allosteric pocket on human hsp70 reveals a mode of inhibition of this therapeutically important protein.
Rodina et al. (2013)
4 more