› 1a4h

X-ray diffraction
2.5Å resolution

STRUCTURE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE IN COMPLEX WITH GELDANAMYCIN

Released:
DOI: 10.2210/pdb1a4h/pdb
PDB entry 1a4h coloured by chain, front view.
PDB entry 1a4h coloured by chain, side view.
PDB entry 1a4h coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.
Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH
Cell 90 65-75 (1997)
PMID: 9230303

Function and Biology Details

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

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: 230 amino acids
Theoretical weight: 26.13 KDa
Source organism: Saccharomyces cerevisiae
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 GDM 1 x GDM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P4322
Unit cell:
a: 74.12Å b: 74.12Å c: 111.35Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 not available

Quick links

Citations

164 review citations

The Hsp70 and Hsp60 chaperone machines.
Bukau et al. (1998)
163 more

9 mentions without citation

Natural Product Inspired N-Terminal Hsp90 Inhibitors: From Bench to Bedside?
Khandelwal et al. (2016)
8 more