PDBe 1us7

X-ray diffraction
2.3Å resolution

Complex of Hsp90 and P50

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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
Hsp90 co-chaperone Cdc37, N-terminally processed Chain: B
Molecule details ›
Chain: B
Length: 265 amino acids
Theoretical weight: 30.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16543 (Residues: 127-378; Coverage: 67%)
Gene names: CDC37, CDC37A
Sequence domains:
Structure domains: Methane Monooxygenase Hydroxylase; Chain G, domain 1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 83.759Å b: 83.759Å c: 148.445Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.188 0.185 0.241
Expression system: Escherichia coli