› 1kuv

X-ray diffraction
2Å resolution

X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition

Released:
DOI: 10.2210/pdb1kuv/pdb
PDB entry 1kuv coloured by chain, front view.
PDB entry 1kuv coloured by chain, side view.
PDB entry 1kuv coloured by chain, top view.
Source organism: Ovis aries
Primary publication:
X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition.
Wolf E, De Angelis J, Khalil EM, Cole PA, Burley SK
J Mol Biol 317 215-24 (2002)
PMID: 11902838

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + a 2-arylethylamine = CoA + an N-acetyl-2-arylethylamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serotonin N-acetyltransferase Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 23.11 KDa
Source organism: Ovis aries
Expression system: Escherichia coli
UniProt:
  • Canonical: Q29495 (Residues: 1-207; Coverage: 100%)
Gene names: AANAT, SNAT
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand CA5 1 x CA5
1 bound ligand:
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25, CHESS BEAMLINE F1
Spacegroup: C2221
Unit cell:
a: 53.313Å b: 68.716Å c: 89.725Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.203 0.25
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structure and functions of the GNAT superfamily of acetyltransferases.
Vetting et al. (2005)
2 more

6 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
5 more