› 3b28

X-ray diffraction
1.35Å resolution

Hsp90 alpha N-terminal domain in complex with an inhibitor CH5015765

Released:
DOI: 10.2210/pdb3b28/pdb
PDB entry 3b28 coloured by chain, front view.
PDB entry 3b28 coloured by chain, side view.
PDB entry 3b28 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-139817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chains: A, B
Molecule details ›
Chains: A, B
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

3 bound ligands:
Ligand GOL 1 x GOL
Ligand B2X 2 x B2X
Ligand MG 2 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 106.98Å b: 98.81Å c: 64.18Å
α: 90° β: 124.43° γ: 90°
R-values:
R R work R free
0.164 0.163 0.181
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

Prediction of Ordered Water Molecules in Protein Binding Sites from Molecular Dynamics Simulations: The Impact of Ligand Binding on Hydration Networks.
Rudling et al. (2018)
3 more