› 1n5r

X-ray diffraction
2.25Å resolution

Crystal structure of the mouse acetylcholinesterase-propidium complex

Released:
DOI: 10.2210/pdb1n5r/pdb
PDB entry 1n5r coloured by chain, front view.
PDB entry 1n5r coloured by chain, side view.
PDB entry 1n5r coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
Bourne Y, Taylor P, Radić Z, Marchot P
EMBO J 22 1-12 (2003)
PMID: 12505979

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
Molecule details ›
Chains: A, B
Length: 543 amino acids
Theoretical weight: 59.76 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: P21836 (Residues: 32-574; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: alpha/beta hydrolase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
5 bound ligands:
Ligand NAG 2 x NAG
Ligand P6G 1 x P6G
Ligand PRM 1 x PRM
Ligand ACY 2 x ACY
Ligand PG4 1 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 79.552Å b: 111.665Å c: 226.834Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.227
Expression system: Homo sapiens

Quick links

Citations

25 review citations

The growing impact of click chemistry on drug discovery.
Kolb et al. (2003)
24 more

7 mentions without citation

Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site.
Bourne et al. (2003)
6 more