› 2wer

X-ray diffraction
1.6Å resolution

Yeast Hsp90 N-terminal domain LI-IV mutant with Radicicol

Released:
DOI: 10.2210/pdb2wer/pdb
PDB entry 2wer coloured by chain, front view.
PDB entry 2wer coloured by chain, side view.
PDB entry 2wer coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural basis of the radicicol resistance displayed by a fungal hsp90.
Prodromou C, Nuttall JM, Millson SH, Roe SM, Sim TS, Tan D, Workman P, Pearl LH, Piper PW
ACS Chem Biol 4 289-97 (2009)
PMID: 19236053

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 220 amino acids
Theoretical weight: 24.86 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P02829 (Residues: 1-220; Coverage: 31%)
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 RDC 2 x RDC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P2221
Unit cell:
a: 74.007Å b: 74.053Å c: 110.193Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.245 0.243 0.273
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Targeting the dynamic HSP90 complex in cancer.
Trepel et al. (2010)
7 more

3 mentions without citation

Drug candidate identification based on gene expression of treated cells using tensor decomposition-based unsupervised feature extraction for large-scale data.
Taguchi YH. (2019)
2 more