› 3b24

X-ray diffraction
1.7Å resolution

Hsp90 alpha N-terminal domain in complex with an aminotriazine fragment molecule

Released:
DOI: 10.2210/pdb3b24/pdb
PDB entry 3b24 coloured by chain, front view.
PDB entry 3b24 coloured by chain, side view.
PDB entry 3b24 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

2 bound ligands:
Ligand MG 1 x MG
Ligand B2J 2 x B2J
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21212
Unit cell:
a: 64.193Å b: 88.51Å c: 98.523Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.161 0.188
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Two-dimensional NMR lineshape analysis of single, multiple, zero and double quantum correlation experiments.
Waudby et al. (2020)
1 more