X-ray diffraction
1.9Å resolution

Structure Of The Hsp90 Inhibitor 7-O-carbamoylpremacbecin Bound To The N- Terminus Of Yeast Hsp90


Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
ATP-dependent molecular chaperone HSP82 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 214 amino acids
Theoretical weight: 24.21 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
  • 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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 104.193Å b: 104.785Å c: 109.913Å
α: 90° β: 89.98° γ: 90°
R R work R free
0.19 0.188 0.226
Expression system: Escherichia coli