› 2pqt

X-ray diffraction
1.78Å resolution

Human N-acetyltransferase 1

Released:
DOI: 10.2210/pdb2pqt/pdb
PDB entry 2pqt coloured by chain, front view.
PDB entry 2pqt coloured by chain, side view.
PDB entry 2pqt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of substrate-binding specificity of human arylamine N-acetyltransferases.
Wu H, Dombrovsky L, Tempel W, Martin F, Loppnau P, Goodfellow GH, Grant DM, Plotnikov AN
J Biol Chem 282 30189-97 (2007)
PMID: 17656365

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148373 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylamine N-acetyltransferase 1 Chain: A
Molecule details ›
Chain: A
Length: 295 amino acids
Theoretical weight: 34.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18440 (Residues: 2-290; Coverage: 100%)
Gene names: AAC1, NAT1
Sequence domains: N-acetyltransferase
Structure domains: Arylamine N-acetyltransferase fold

Ligands and Environments

2 bound ligands:
Ligand CL 1 x CL
Ligand UNX 2 x UNX
1 modified residue:
Ligand TYX 1 x TYX

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P21
Unit cell:
a: 37.274Å b: 44.975Å c: 83.959Å
α: 90° β: 99.17° γ: 90°
R-values:
R R work R free
0.173 0.17 0.216
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Arylamine N-acetyltransferases: structural and functional implications of polymorphisms.
Sim et al. (2008)
12 more

13 mentions without citation

Structure/function evaluations of single nucleotide polymorphisms in human N-acetyltransferase 2.
Walraven et al. (2008)
12 more