1ah8

X-ray diffraction
2.1Å resolution

STRUCTURE OF THE ORTHORHOMBIC FORM OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 24.87 KDa
Source organism: Saccharomyces cerevisiae
UniProt:
  • Canonical: P02829 (Residues: 1-220; Coverage: 31%)
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: P212121
Unit cell:
a: 115.54Å b: 112.9Å c: 44.72Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.196 0.255