› 2iws

X-ray diffraction
2.7Å 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 Chain: A
Molecule details ›
Chain: A
Length: 214 amino acids
Theoretical weight: 24.21 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 1-214; Coverage: 30%)
Gene names: HSP82, HSP90, YPL240C
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand NP4 1 x NP4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P4322
Unit cell:
a: 73.841Å b: 73.841Å c: 109.135Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.295
Expression system: Escherichia coli

Quick links

Citations

8 review citations

New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.
Li et al. (2009)
7 more

3 mentions without citation

The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts.
Spichty et al. (2009)
2 more