› 3wha

X-ray diffraction
1.3Å resolution

Hsp90 alpha N-terminal domain in complex with a tricyclic inhibitor

Released:
DOI: 10.2210/pdb3wha/pdb
PDB entry 3wha coloured by chain, front view.
PDB entry 3wha coloured by chain, side view.
PDB entry 3wha coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of 2-amino-6-(1H,3H-benzo[de]isochromen-6-yl)-1,3,5-triazines as novel Hsp90 inhibitors.
Suda A, Kawasaki K, Komiyama S, Isshiki Y, Yoon DO, Kim SJ, Na YJ, Hasegawa K, Fukami TA, Sato S, Miura T, Ono N, Yamazaki T, Saitoh R, Shimma N, Shiratori Y, Tsukuda T
Bioorg Med Chem 22 892-905 (2014)
PMID: 24369839

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
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139824 (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 WHA 2 x WHA
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2
Unit cell:
a: 107.17Å b: 98.92Å c: 64.24Å
α: 90° β: 124.55° γ: 90°
R-values:
R R work R free
0.185 0.184 0.2
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Targeting HSP90 as a Novel Therapy for Cancer: Mechanistic Insights and Translational Relevance.
Zhang et al. (2022)
1 more

1 mention without citation

Network pharmacology- and molecular docking-based investigation of the therapeutic potential and mechanism of daucosterol against multiple myeloma.
Zeng et al. (2023)