› 1l0c

X-ray diffraction
2.3Å resolution

Investigation of the Roles of Catalytic Residues in Serotonin N-Acetyltransferase

Released:
DOI: 10.2210/pdb1l0c/pdb
PDB entry 1l0c coloured by chain, front view.
PDB entry 1l0c coloured by chain, side view.
PDB entry 1l0c coloured by chain, top view.
Source organism: Ovis aries
Primary publication:
Investigation of the roles of catalytic residues in serotonin N-acetyltransferase.
Scheibner KA, De Angelis J, Burley SK, Cole PA
J Biol Chem 277 18118-26 (2002)
PMID: 11884405

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: 23.1 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 COT 1 x COT
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: C2221
Unit cell:
a: 53.21Å b: 68.681Å c: 89.422Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.193 0.246
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

3 mentions without citation

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