› 6arx

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

Released:
DOI: 10.2210/pdb6arx/pdb
PDB entry 6arx coloured by chain, front view.
PDB entry 6arx coloured by chain, side view.
PDB entry 6arx coloured by chain, top view.
Source organism: Anopheles gambiae
Primary publication:
Structure of the G119S Mutant Acetylcholinesterase of the Malaria Vector Anopheles gambiae Reveals Basis of Insecticide Resistance.
Cheung J, Mahmood A, Kalathur R, Liu L, Carlier PR
Structure 26 130-136.e2 (2018)
PMID: 29276037

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183114 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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
UniProt:
  • Canonical: Q869C3 (Residues: 162-702; Coverage: 77%)
Gene names: ACE1, ACHE1, AGAP001356, Ace
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

3 bound ligands:
Ligand NAG 3 x NAG
Ligand FLC 4 x FLC
Ligand CL 1 x CL
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-values:
R R work R free
0.179 0.178 0.203
Expression system: Spodoptera frugiperda

Quick links

Citations

4 review citations

Anopheles metabolic proteins in malaria transmission, prevention and control: a review.
Adedeji et al. (2020)
3 more

7 mentions without citation

Dynamic Roles of Insect Carboxyl/Cholinesterases in Chemical Adaptation.
Cruse et al. (2023)
6 more