X-ray diffraction
2.6Å resolution

Structures of ligand bound human choline acetyltransferase provide insight into regulation of acetylcholine synthesis

Source organism: Homo sapiens
Entry authors: Kim AR, Rylett RJ, Shilton BH

Function and Biology Details

Reaction catalysed:
Acetyl-CoA + choline = CoA + O-acetylcholine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Choline O-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 612 amino acids
Theoretical weight: 68.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P28329 (Residues: 120-733; Coverage: 82%)
Gene name: CHAT
Sequence domains: Choline/Carnitine o-acyltransferase
Structure domains:

Ligands and Environments

Cofactor: Ligand SOP 1 x SOP
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 55.27Å b: 74.03Å c: 165.83Å
α: 90° β: 90° γ: 90°
R R work R free
0.276 0.237 0.285
Expression system: Escherichia coli BL21(DE3)