3t0h

X-ray diffraction
1.2Å resolution

Structure insights into mechanisms of ATP hydrolysis and the activation of human Hsp90

Released:
Source organism: Homo sapiens
Primary publication:
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.
Acta Biochim Biophys Sin (Shanghai) 44 300-6 (2012)
PMID: 22318716

Function and Biology Details

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-139817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chain: A
Molecule details ›
Chain: A
Length: 228 amino acids
Theoretical weight: 25.66 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07900 (Residues: 9-236; Coverage: 31%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: I222
Unit cell:
a: 65.287Å b: 88.934Å c: 99.672Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.171
Expression system: Escherichia coli