1am1

X-ray diffraction
2Å resolution

ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent molecular chaperone HSP82 Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 24.08 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 2-214; 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.5
Spacegroup: P4322
Unit cell:
a: 73.91Å b: 73.91Å c: 110.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Escherichia coli