› 2fy5

X-ray diffraction
2.6Å resolution

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

Released:
DOI: 10.2210/pdb2fy5/pdb
PDB entry 2fy5 coloured by chain, front view.
PDB entry 2fy5 coloured by chain, side view.
PDB entry 2fy5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Substrate binding and catalytic mechanism of human choline acetyltransferase.
Kim AR, Rylett RJ, Shilton BH
Biochemistry 45 14621-31 (2006)
PMID: 17144655

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151207 (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
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-values:
R R work R free
0.276 0.237 0.285
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

What have we learned from the congenital myasthenic syndromes.
Engel et al. (2010)
2 more