› 1hk7

X-ray diffraction
2.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136252 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent molecular chaperone HSP82 Chains: A, B
Molecule details ›
Chains: A, B
Length: 288 amino acids
Theoretical weight: 33.87 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 273-560; Coverage: 41%)
Gene names: HSP82, HSP90, YPL240C
Sequence domains: Hsp90 protein
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CD 6 x CD
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P61
Unit cell:
a: 112.879Å b: 112.879Å c: 112.059Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.24 0.277
Expression system: Escherichia coli

Quick links

Citations

74 review citations

HSP90 and the chaperoning of cancer.
Whitesell et al. (2005)
73 more

9 mentions without citation

The 'active life' of Hsp90 complexes.
Prodromou C. (2012)
8 more