5dtj

X-ray diffraction
2.71Å resolution

Crystal Structure of dfp-inhibited mouse acetylcholinesterase in complex with the reactivator SP-134

Released:

Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 545 amino acids
Theoretical weight: 60.13 KDa
Source organism: Mus musculus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P21836 (Residues: 32-573; Coverage: 93%)
Gene name: Ache
Sequence domains: Carboxylesterase family
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 79.487Å b: 113.367Å c: 227.117Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.179 0.221
Expression system: Trichoplusia ni