› 2cgf

X-ray diffraction
2.2Å resolution

A RADICICOL ANALOGUE BOUND TO THE ATP BINDING SITE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE

Released:
DOI: 10.2210/pdb2cgf/pdb
PDB entry 2cgf coloured by chain, front view.
PDB entry 2cgf coloured by chain, side view.
PDB entry 2cgf coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Inhibition of Hsp90 with synthetic macrolactones: synthesis and structural and biological evaluation of ring and conformational analogs of radicicol.
Proisy N, Sharp SY, Boxall K, Connelly S, Roe SM, Prodromou C, Slawin AM, Pearl LH, Workman P, Moody CJ
Chem Biol 13 1203-15 (2006)
PMID: 17114002

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136258 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ATP-dependent molecular chaperone HSP82 Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 25.5 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 1-214; Coverage: 30%)
Gene names: HSP82, HSP90, YPL240C
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 P2N 1 x P2N
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P4322
Unit cell:
a: 73.654Å b: 73.654Å c: 110.733Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.168 0.208
Expression system: Escherichia coli

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Citations

8 review citations

New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.
Li et al. (2009)
7 more

1 mention without citation

The HSP90 binding mode of a radicicol-like E-oxime determined by docking, binding free energy estimations, and NMR 15N chemical shifts.
Spichty et al. (2009)