› 3fe1

X-ray diffraction
2.2Å resolution

Crystal structure of the human 70kDa heat shock protein 6 (Hsp70B') ATPase domain in complex with ADP and inorganic phosphate

Released:
DOI: 10.2210/pdb3fe1/pdb
PDB entry 3fe1 coloured by chain, front view.
PDB entry 3fe1 coloured by chain, side view.
PDB entry 3fe1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.
Wisniewska M, Karlberg T, Lehtiö L, Johansson I, Kotenyova T, Moche M, Schüler H
PLoS One 5 e8625 (2010)
PMID: 20072699

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-147863 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock 70 kDa protein 6 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 403 amino acids
Theoretical weight: 44.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P17066 (Residues: 6-385; Coverage: 59%)
Gene names: HSP70B', HSPA6
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand ADP 3 x ADP
Ligand PO4 3 x PO4
Ligand MG 3 x MG
Ligand CL 1 x CL
Ligand PGE 1 x PGE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 236.45Å b: 105.4Å c: 73.59Å
α: 90° β: 101.04° γ: 90°
R-values:
R R work R free
0.201 0.199 0.238
Expression system: Escherichia coli

Quick links

Citations

11 review citations

HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
Stricher et al. (2013)
10 more

6 mentions without citation

Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.
Wisniewska et al. (2010)
5 more