3t10

X-ray diffraction
1.24Å resolution

HSP90 N-terminal domain bound to ACP

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

Assembly composition:
monomeric (preferred)
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

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 53.17Å b: 44.972Å c: 53.854Å
α: 90° β: 115.15° γ: 90°
R-values:
R R work R free
0.158 0.158 0.172
Expression system: Escherichia coli