› 1w6f

X-ray diffraction
2.1Å resolution

Arylamine N-acetyltransferase from Mycobacterium smegmatis with the anti-tubercular drug isoniazid bound in the active site.

Released:
DOI: 10.2210/pdb1w6f/pdb
PDB entry 1w6f coloured by chain, front view.
PDB entry 1w6f coloured by chain, side view.
PDB entry 1w6f coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis
Primary publication:
Binding of the anti-tubercular drug isoniazid to the arylamine N-acetyltransferase protein from Mycobacterium smegmatis.
Sandy J, Holton S, Fullam E, Sim E, Noble M
Protein Sci 14 775-82 (2005)
PMID: 15722451

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + an arylamine = CoA + an N-acetylarylamine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131467 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arylamine N-acetyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 278 amino acids
Theoretical weight: 30.57 KDa
Source organism: Mycolicibacterium smegmatis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O86309 (Residues: 1-275; Coverage: 100%)
Gene name: nat
Sequence domains: N-acetyltransferase
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ISZ 4 x ISZ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 101.208Å b: 106.039Å c: 140.362Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.18 0.219
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Arylamine N-acetyltransferases: what we learn from genes and genomes.
Boukouvala et al. (2005)
8 more

5 mentions without citation

Arylamine N-acetyltransferases: a structural perspective.
Zhou et al. (2013)
4 more