PDBe 1vzj

X-ray diffraction
2.35Å resolution

Structure of the tetramerization domain of acetylcholinesterase: four-fold interaction of a WWW motif with a left-handed polyproline helix

Released:

Function and Biology Details

Reaction catalysed:
Acetylcholine + H(2)O = choline + acetate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Acetylcholinesterase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 40 amino acids
Theoretical weight: 5.13 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P22303 (Residues: 575-614; Coverage: 7%)
Gene name: ACHE
Sequence domains: Acetylcholinesterase tetramerisation domain
Acetylcholinesterase collagenic tail peptide Chains: I, J
Molecule details ›
Chains: I, J
Length: 15 amino acids
Theoretical weight: 1.68 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y215 (Residues: 53-67; Coverage: 4%)
Gene name: COLQ

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21
Unit cell:
a: 53.73Å b: 58.79Å c: 58.8Å
α: 90° β: 111.38° γ: 90°
R-values:
R R work R free
0.247 0.247 0.259
Expression system: Not provided