› 4dmo

X-ray diffraction
2.14Å resolution

Crystal structure of the (BACCR)NAT3 arylamine N-acetyltransferase from Bacillus cereus reveals a unique Cys-His-Glu catalytic triad

Released:
DOI: 10.2210/pdb4dmo/pdb
PDB entry 4dmo coloured by chain, front view.
PDB entry 4dmo coloured by chain, side view.
PDB entry 4dmo coloured by chain, top view.
Source organism: Bacillus cereus ATCC 14579
Primary publication:
Structural and biochemical characterization of an active arylamine N-acetyltransferase possessing a non-canonical Cys-His-Glu catalytic triad.
Kubiak X, Li de la Sierra-Gallay I, Chaffotte AF, Pluvinage B, Weber P, Haouz A, Dupret JM, Rodrigues-Lima F
J Biol Chem 288 22493-505 (2013)
PMID: 23770703

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an N-hydroxyarylamine = CoA + an N-acetoxyarylamine
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-182473 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-hydroxyarylamine O-acetyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 265 amino acids
Theoretical weight: 30.1 KDa
Source organism: Bacillus cereus ATCC 14579
Expression system: Escherichia coli
UniProt:
  • Canonical: Q81AS3 (Residues: 1-263; Coverage: 100%)
Gene name: BC_3483
Sequence domains: N-acetyltransferase
Structure domains: Arylamine N-acetyltransferase fold

Ligands and Environments

1 bound ligand:
Ligand KH2 3 x KH2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: C2
Unit cell:
a: 90.43Å b: 44.52Å c: 132.97Å
α: 90° β: 103.8° γ: 90°
R-values:
R R work R free
0.205 0.202 0.255
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Comparative analysis of xenobiotic metabolising N-acetyltransferases from ten non-human primates as in vitro models of human homologues.
Tsirka et al. (2018)
4 more

7 mentions without citation

Vasohibins: new transglutaminase-like cysteine proteases possessing a non-canonical Cys-His-Ser catalytic triad.
Sanchez-Pulido et al. (2016)
6 more