› 1s3x

X-ray diffraction
1.84Å resolution

The crystal structure of the human Hsp70 ATPase domain

Released:
DOI: 10.2210/pdb1s3x/pdb
PDB entry 1s3x coloured by chain, front view.
PDB entry 1s3x coloured by chain, side view.
PDB entry 1s3x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain.
Sriram M, Osipiuk J, Freeman B, Morimoto R, Joachimiak A
Structure 5 403-14 (1997)
PMID: 9083109

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: 382 amino acids
Theoretical weight: 42.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 1-382; Coverage: 60%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand PO4 1 x PO4
Ligand CA 2 x CA
Ligand NA 2 x NA
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 145.47Å b: 63.34Å c: 45.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.219
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Chaperone-mediated protein folding.
Fink AL. (1999)
12 more

26 mentions without citation

Exosomal mediated signal transduction through artificial microRNA (amiRNA): A potential target for inhibition of SARS-CoV-2.
Vadivalagan et al. (2022)
25 more