5hfa

X-ray diffraction
2.2Å resolution

Crystal structure of human acetylcholinesterase in complex with paraoxon and 2-PAM

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
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 542 amino acids
Theoretical weight: 59.45 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P22303 (Residues: 33-574; Coverage: 93%)
Gene name: ACHE
Sequence domains: Carboxylesterase family
Structure domains: Rossmann fold

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P3121
Unit cell:
a: 104.803Å b: 104.803Å c: 323.462Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.181 0.224
Expression system: Homo sapiens