› 2vbq

X-ray diffraction
2Å resolution

Structure of AAC(6')-Iy in complex with bisubstrate analog CoA-S- monomethyl-acetylneamine.

Released:
DOI: 10.2210/pdb2vbq/pdb
PDB entry 2vbq coloured by chain, front view.
PDB entry 2vbq coloured by chain, side view.
PDB entry 2vbq coloured by chain, top view.
Source organism: Salmonella enterica
Primary publication:
Kinetic and structural analysis of bisubstrate inhibition of the Salmonella enterica aminoglycoside 6'-N-acetyltransferase.
Magalhães ML, Vetting MW, Gao F, Freiburger L, Auclair K, Blanchard JS
Biochemistry 47 579-84 (2008)
PMID: 18095712

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 165 amino acids
Theoretical weight: 18.56 KDa
Source organism: Salmonella enterica
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 BSJ 2 x BSJ
2 bound ligands:
Ligand NI 1 x NI
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: C2
Unit cell:
a: 84.964Å b: 44.599Å c: 88.387Å
α: 90° β: 93.92° γ: 90°
R-values:
R R work R free
0.183 0.181 0.23
Expression system: Escherichia coli

Quick links

Citations

6 review citations

The future of aminoglycosides: the end or renaissance?
Houghton et al. (2010)
5 more

7 mentions without citation

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