› 1uym

X-ray diffraction
2.45Å resolution

Human Hsp90-beta with PU3 (9-Butyl-8(3,4,5-trimethoxy-benzyl)-9H-purin-6-ylamine)

Released:
DOI: 10.2210/pdb1uym/pdb
PDB entry 1uym coloured by chain, front view.
PDB entry 1uym coloured by chain, side view.
PDB entry 1uym coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-activity relationships in purine-based inhibitor binding to HSP90 isoforms.
Wright L, Barril X, Dymock B, Sheridan L, Surgenor A, Beswick M, Drysdale M, Collier A, Massey A, Davies N, Fink A, Fromont C, Aherne W, Boxall K, Sharp S, Workman P, Hubbard RE
Chem Biol 11 775-85 (2004)
PMID: 15217611

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140046 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-beta Chain: A
Molecule details ›
Chain: A
Length: 220 amino acids
Theoretical weight: 24.67 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P08238 (Residues: 2-221; Coverage: 30%)
Gene names: HSP90AB1, HSP90B, HSPC2, HSPC3, HSPCB
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 PU3 1 x PU3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I222
Unit cell:
a: 66.861Å b: 90.707Å c: 96.289Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.238 0.235 0.294
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

25 review citations

Hsp90 molecular chaperone inhibitors: are we there yet?
Neckers et al. (2012)
24 more

20 mentions without citation

Discovery and development of heat shock protein 90 inhibitors.
Taldone et al. (2009)
19 more