› 3o0i

X-ray diffraction
1.47Å resolution

Structure of the human Hsp90-alpha N-domain bound to the hsp90 inhibitor PU-H54

Released:
DOI: 10.2210/pdb3o0i/pdb
PDB entry 3o0i coloured by chain, front view.
PDB entry 3o0i coloured by chain, side view.
PDB entry 3o0i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Paralog-selective Hsp90 inhibitors define tumor-specific regulation of HER2.
Patel PD, Yan P, Seidler PM, Patel HJ, Sun W, Yang C, Que NS, Taldone T, Finotti P, Stephani RA, Gewirth DT, Chiosis G
Nat Chem Biol 9 677-84 (2013)
PMID: 23995768

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: 256 amino acids
Theoretical weight: 28.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07900 (Residues: 1-236; Coverage: 32%)
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

1 bound ligand:
Ligand P54 1 x P54
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: I222
Unit cell:
a: 66.711Å b: 90.881Å c: 98.603Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

38 review citations

Glucose-regulated proteins in cancer: molecular mechanisms and therapeutic potential.
Lee AS. (2014)
37 more

10 mentions without citation

Paralog Specific Hsp90 Inhibitors - A Brief History and a Bright Future.
Gewirth DT. (2016)
9 more