› 3t0z

X-ray diffraction
2.19Å resolution

Hsp90 N-terminal domain bound to ATP

Released:
DOI: 10.2210/pdb3t0z/pdb
PDB entry 3t0z coloured by chain, front view.
PDB entry 3t0z coloured by chain, side view.
PDB entry 3t0z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90.
Li J, Sun L, Xu C, Yu F, Zhou H, Zhao Y, Zhang J, Cai J, Mao C, Tang L, Xu Y, He J
Acta Biochim Biophys Sin (Shanghai) 44 300-6 (2012)
PMID: 22318716

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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:
Ligand ATP 1 x ATP
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 50.709Å b: 46.78Å c: 53.223Å
α: 90° β: 111.59° γ: 90°
R-values:
R R work R free
0.206 0.201 0.258
Expression system: Escherichia coli

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Citations

2 review citations

Targeting heat-shock-protein 90 (Hsp90) by natural products: geldanamycin, a show case in cancer therapy.
Franke et al. (2013)
1 more

15 mentions without citation

Structural Basis of Parasitic HSP90 ATPase Inhibition by Small Molecules.
Tassone et al. (2022)
14 more