› 1hjo

X-ray diffraction
2.3Å resolution

ATPase domain of human heat shock 70kDa protein 1

Released:
DOI: 10.2210/pdb1hjo/pdb
PDB entry 1hjo coloured by chain, front view.
PDB entry 1hjo coloured by chain, side view.
PDB entry 1hjo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a new crystal form of human Hsp70 ATPase domain.
Osipiuk J, Walsh MA, Freeman BC, Morimoto RI, Joachimiak A
Acta Crystallogr D Biol Crystallogr 55 1105-7 (1999)
PMID: 10216320

Function and Biology Details

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-143649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock 70 kDa protein 1A Chain: A
Molecule details ›
Chain: A
Length: 380 amino acids
Theoretical weight: 41.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 3-382; Coverage: 59%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 1 x CA
Ligand CL 1 x CL
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P212121
Unit cell:
a: 70.215Å b: 72.564Å c: 98.927Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.253
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

18 mentions without citation

Mechanisms for regulation of Hsp70 function by Hsp40.
Fan et al. (2003)
17 more