PDBe 2fy4

X-ray diffraction
2.3Å resolution

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

Released:
Source organism: Homo sapiens
Primary publication:
Substrate binding and catalytic mechanism of human choline acetyltransferase.
Biochemistry 45 14621-31 (2006)
PMID: 17144655

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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)
UniProt:
  • Canonical: P28329 (Residues: 120-733; Coverage: 82%)
Gene name: CHAT

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 54.7Å b: 73.98Å c: 165.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.203 0.24
Expression system: Escherichia coli BL21(DE3)