› 3atu

X-ray diffraction
1.65Å resolution

Crystal structure of human Hsp70 NBD in the ADP- and Mg ion-bound state

Released:
DOI: 10.2210/pdb3atu/pdb
PDB entry 3atu coloured by chain, front view.
PDB entry 3atu coloured by chain, side view.
PDB entry 3atu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Biochemical and structural studies on the high affinity of Hsp70 for ADP.
Arakawa A, Handa N, Shirouzu M, Yokoyama S
Protein Sci 20 1367-79 (2011)
PMID: 21608060

Function and Biology Details

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

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: 392 amino acids
Theoretical weight: 43.15 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 1-388; Coverage: 61%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ADP 1 x ADP
Ligand PO4 1 x PO4
Ligand MG 1 x MG
Ligand NA 1 x NA
Ligand PG0 1 x PG0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 46.114Å b: 63.675Å c: 143.534Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.186 0.218
Expression system: Escherichia coli

Quick links

Citations

10 review citations

The human HSP70 family of chaperones: where do we stand?
Radons J. (2016)
9 more

11 mentions without citation

Biochemical and structural studies on the high affinity of Hsp70 for ADP.
Arakawa et al. (2011)
10 more