X-ray diffraction
2.3Å resolution

Crystal structure of an insecticide-resistant acetylcholinesterase mutant from the malaria vector Anopheles gambiae in the ligand-free state


Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 542 amino acids
Theoretical weight: 60.62 KDa
Source organism: Anopheles gambiae
Expression system: Spodoptera frugiperda
  • Canonical: Q869C3 (Residues: 162-702; Coverage: 77%)
Gene names: ACE1, ACHE1, AGAP001356, Ace
Sequence domains: Carboxylesterase family

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P61
Unit cell:
a: 149.599Å b: 149.599Å c: 225.857Å
α: 90° β: 90° γ: 120°
R R work R free
0.179 0.178 0.203
Expression system: Spodoptera frugiperda