› 1s60

X-ray diffraction
3Å resolution

Aminoglycoside N-Acetyltransferase AAC(6')-Iy in Complex with CoA and N-terminal His(6)-tag (crystal form 2)

Released:
DOI: 10.2210/pdb1s60/pdb
PDB entry 1s60 coloured by chain, front view.
PDB entry 1s60 coloured by chain, side view.
PDB entry 1s60 coloured by chain, top view.
Source organism: Salmonella enterica subsp. enterica serovar Enteritidis
Primary publication:
A bacterial acetyltransferase capable of regioselective N-acetylation of antibiotics and histones.
Vetting MW, Magnet S, Nieves E, Roderick SL, Blanchard JS
Chem Biol 11 565-73 (2004)
PMID: 15123251

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + kanamycin-B = CoA + N(6')-acetylkanamycin-B
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoglycoside N(6')-acetyltransferase type 1 Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.56 KDa
Source organism: Salmonella enterica subsp. enterica serovar Enteritidis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9R381 (Residues: 1-145; Coverage: 100%)
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 1 x COA
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3221
Unit cell:
a: 84.6Å b: 84.6Å c: 66.75Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.225 0.225 0.267
Expression system: Escherichia coli

Quick links

Citations

14 review citations

The antibiotic resistome: the nexus of chemical and genetic diversity.
Wright GD. (2007)
13 more

5 mentions without citation

Aminoglycoside modifying enzymes.
Ramirez et al. (2010)
4 more