› 3b25

X-ray diffraction
1.75Å resolution

Hsp90 alpha N-terminal domain in complex with an inhibitor CH4675194

Released:
DOI: 10.2210/pdb3b25/pdb
PDB entry 3b25 coloured by chain, front view.
PDB entry 3b25 coloured by chain, side view.
PDB entry 3b25 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Lead generation of heat shock protein 90 inhibitors by a combination of fragment-based approach, virtual screening, and structure-based drug design.
Miura T, Fukami TA, Hasegawa K, Ono N, Suda A, Shindo H, Yoon DO, Kim SJ, Na YJ, Aoki Y, Shimma N, Tsukuda T, Shiratori Y
Bioorg Med Chem Lett 21 5778-83 (2011)
PMID: 21875802

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-530348 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 25.79 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

1 bound ligand:
Ligand B2K 1 x B2K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: I222
Unit cell:
a: 66.788Å b: 91.112Å c: 98.746Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.203
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Targeting protein-protein interactions as an anticancer strategy.
Ivanov et al. (2013)
1 more

4 mentions without citation

Efficient Synthesis and Docking Studies of Novel Benzothiazole-Based Pyrimidinesulfonamide Scaffolds as New Antiviral Agents and Hsp90α Inhibitors.
Azzam et al. (2020)
3 more