› 1maa

X-ray diffraction
2.9Å resolution

MOUSE ACETYLCHOLINESTERASE CATALYTIC DOMAIN, GLYCOSYLATED PROTEIN

Released:
DOI: 10.2210/pdb1maa/pdb
PDB entry 1maa coloured by chain, front view.
PDB entry 1maa coloured by chain, side view.
PDB entry 1maa coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Crystal structure of mouse acetylcholinesterase. A peripheral site-occluding loop in a tetrameric assembly.
Bourne Y, Taylor P, Bougis PE, Marchot P
J Biol Chem 274 2963-70 (1999)
PMID: 9915834

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149441 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 547 amino acids
Theoretical weight: 60.28 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-578; Coverage: 94%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
4 bound ligands:
Ligand NAG 1 x NAG
Ligand DME 4 x DME
Ligand GOL 4 x GOL
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P212121
Unit cell:
a: 136.55Å b: 173.13Å c: 224.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.248
Expression system: Homo sapiens

Quick links

Citations

13 review citations

Structural roles of acetylcholinesterase variants in biology and pathology.
Grisaru et al. (1999)
12 more

12 mentions without citation

How to build a central synapse: clues from cell culture.
Craig et al. (2006)
11 more