4asg

X-ray diffraction
2.2Å resolution

The structure of modified benzoquinone ansamycins bound to yeast N- terminal Hsp90

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: 220 amino acids
Theoretical weight: 24.87 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P4322
Unit cell:
a: 74.126Å b: 74.126Å c: 110.177Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.241
Expression system: Escherichia coli