5ydh

X-ray diffraction
3.21Å resolution

Crystal structure of acetylcholinesterase catalytic subunits of the malaria vector anopheles gambiae, 3.2 A

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

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
Macromolecules (3 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 576 amino acids
Theoretical weight: 64.39 KDa
Source organism: Anopheles gambiae
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q869C3 (Residues: 162-737; Coverage: 82%)
Gene names: ACE1, ACHE1, AGAP001356, Ace
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P61
Unit cell:
a: 148.659Å b: 148.659Å c: 226.021Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.207 0.231
Expression system: Komagataella pastoris