Inhibition of the HSP90 molecular chaperone in vitro and in vivo by novel, synthetic, potent resorcinylic pyrazole, isoxazole amide analogs

Structure

x-ray diffraction · resolution 1.9 · 1 distinct chain · 43% helix, 23% strand (DSSP).

Ligands and binding sites

• 2GG · 5-(5-chloro-2,4-dihydroxyphenyl)-N-ethyl-4-(4-methoxyphenyl)isoxazole-3-carboxamide · ligand · chains A
• MG · Magnesium ion · metal · 2 copies · chains A
• SO4 · Sulfate ion · ion · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Compared structures

• 2UWD · Inhibition of the HSP90 molecular chaperone in vitro and in vivo by novel, synthetic… · the same entry in another collection · chain A against A, TM-score 1.00
• P07900 · AlphaFold monomer V2.0 prediction for heat shock protein HSP 90-alpha (P07900) · a predicted model of the same protein · chain A against A, TM-score 0.82

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P07900
• Elsewhere: RCSB PDB 2UWD · PDBe 2UWD · UniProt P07900