› 4qww

X-ray diffraction
2.7Å resolution

Function and Biology Details

Reaction catalysed: 
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212667 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (5 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 542 amino acids
Theoretical weight: 60.32 KDa
Source organism: Bungarus fasciatus
UniProt:
  • Canonical: Q92035 (Residues: 32-573; Coverage: 94%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase
Fab410 antibody light chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 213 amino acids
Theoretical weight: 23.29 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Fab410 antibody heavy chain Chains: D, F
Molecule details ›
Chains: D, F
Length: 234 amino acids
Theoretical weight: 25.35 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
2 bound ligands:
Ligand EDO 2 x EDO
Ligand NAG 1 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21212
Unit cell:
a: 156.592Å b: 251.336Å c: 73.978Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.201 0.199 0.239

Quick links

Citations

4 review citations

A Comprehensive Review of Cholinesterase Modeling and Simulation.
De Boer et al. (2021)
3 more

7 mentions without citation

Hot Spots for Protein Partnerships at the Surface of Cholinesterases and Related α/β Hydrolase Fold Proteins or Domains-A Structural Perspective.
Bourne et al. (2017)
6 more