› 2wi1

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chain: A
Molecule details ›
Chain: A
Length: 236 amino acids
Theoretical weight: 26.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07900 (Residues: 1-236; Coverage: 32%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

2 bound ligands:
Ligand MG 1 x MG
Ligand ZZ2 1 x ZZ2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I222
Unit cell:
a: 64.978Å b: 89.611Å c: 99.714Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.27 0.267 0.321
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

20 review citations

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

1 mention without citation

Co-crystalization and in vitro biological characterization of 5-aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors.
Sharp et al. (2012)