› 2a4n

X-ray diffraction
2.2Å resolution

Crystal structure of aminoglycoside 6'-N-acetyltransferase complexed with coenzyme A

Released:
DOI: 10.2210/pdb2a4n/pdb
Model geometry
Fit model/data
PDB entry 2a4n coloured by chain, front view.
PDB entry 2a4n coloured by chain, side view.
PDB entry 2a4n coloured by chain, top view.
Source organism: Enterococcus faecium
Primary publication:
Structures of aminoglycoside acetyltransferase AAC(6')-Ii in a novel crystal form: structural and normal-mode analyses.
Burk DL, Xiong B, Breitbach C, Berghuis AM
Acta Crystallogr D Biol Crystallogr 61 1273-9 (2005)
PMID: 16131761

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-175267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetyltransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 182 amino acids
Theoretical weight: 20.73 KDa
Source organism: Enterococcus faecium
Expression system: Escherichia coli str. K-12 substr. W3110
UniProt:
  • Canonical: Q47764 (Residues: 1-182; Coverage: 100%)
Gene name: aac(6')-Ii
Sequence domains: Acetyltransferase (GNAT) family
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand COA 2 x COA
1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X8C
Spacegroup: C2221
Unit cell:
a: 71.48Å b: 127.35Å c: 76.91Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.206 0.255
Expression system: Escherichia coli str. K-12 substr. W3110

Quick links

Citations

2 review citations

Amikacin: Uses, Resistance, and Prospects for Inhibition.
Ramirez et al. (2017)
1 more

9 mentions without citation

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