› 1xqr

X-ray diffraction
2.1Å resolution

Crystal structure of the HspBP1 core domain

Released:
DOI: 10.2210/pdb1xqr/pdb
PDB entry 1xqr coloured by chain, front view.
PDB entry 1xqr coloured by chain, side view.
PDB entry 1xqr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange.
Shomura Y, Dragovic Z, Chang HC, Tzvetkov N, Young JC, Brodsky JL, Guerriero V, Hartl FU, Bracher A
Mol Cell 17 367-79 (2005)
PMID: 15694338

Function and Biology Details

Biochemical function:
  • not assigned
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-192762 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hsp70-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 296 amino acids
Theoretical weight: 33.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NZL4 (Residues: 84-359; Coverage: 77%)
Gene names: HSPBP, HSPBP1, PP1845
Sequence domains: Nucleotide exchange factor Fes1
Structure domains: Leucine-rich Repeat Variant

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: C2
Unit cell:
a: 76.68Å b: 84.286Å c: 89.945Å
α: 90° β: 96° γ: 90°
R-values:
R R work R free
0.213 0.211 0.249
Expression system: Escherichia coli

Quick links

Citations

31 review citations

Molecular chaperones and protein quality control.
Bukau et al. (2006)
30 more

10 mentions without citation

Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates.
Karunanayake et al. (2021)
9 more