› 7d25

X-ray diffraction
1.65Å resolution

Hsp90 alpha N-terminal domain in complex with a 14 compund

Released:
DOI: 10.2210/pdb7d25/pdb
Model geometry
Fit model/data
PDB entry 7d25 coloured by chain, front view.
PDB entry 7d25 coloured by chain, side view.
PDB entry 7d25 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural Basis for Design of New Purine-Based Inhibitors Targeting the Hydrophobic Binding Pocket of Hsp90.
Shin SC, El-Damasy AK, Lee JH, Seo SH, Kim JH, Seo YH, Lee Y, Yu JH, Bang EK, Kim EE, Keum G
OpenAccess logo Int J Mol Sci 21 (2020)
PMID: 33317068

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-139829 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chain: A
Molecule details ›
Chain: A
Length: 215 amino acids
Theoretical weight: 24.11 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07901 (Residues: 16-224; Coverage: 29%)
Gene names: Hsp86, Hsp86-1, Hsp90aa1, Hspca
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase

Ligands and Environments

1 bound ligand:
Ligand GQ6 2 x GQ6
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: I222
Unit cell:
a: 67.604Å b: 89.828Å c: 98.231Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.186 0.214
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Geldanamycin treatment does not result in anti-cancer activity in a preclinical model of orthotopic mesothelioma.
Orozco Morales et al. (2023)

1 mention without citation

Structural Basis for Design of New Purine-Based Inhibitors Targeting the Hydrophobic Binding Pocket of Hsp90.
Shin et al. (2020)