X-ray diffraction
3.45Å resolution

Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector anopheles gambiae, new crystal packing

Source organism: Anopheles gambiae
Entry authors: Han Q, Guan H, Ding H, Liao C, Robinson H, Li J

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Acetylcholinesterase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 553 amino acids
Theoretical weight: 61.68 KDa
Source organism: Anopheles gambiae
Expression system: Komagataella pastoris
  • Canonical: Q869C3 (Residues: 162-714; Coverage: 79%)
Gene names: ACE1, ACHE1, AGAP001356, Ace
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 127.44Å b: 235.91Å c: 167.27Å
α: 90° β: 90° γ: 90°
R R work R free
0.202 0.2 0.242
Expression system: Komagataella pastoris