X-ray diffraction
1.98Å resolution

Inhibition of an antibiotic resistance enzyme: crystal structure of aminoglycoside phosphotransferase APH(2")-ID/APH(2")-IVA in complex with kanamycin inhibited with quercetin


Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
APH domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 322 amino acids
Theoretical weight: 38.28 KDa
Source organism: Enterococcus casseliflavus
Expression system: Escherichia coli BL21(DE3)
  • Canonical: O68183 (Residues: 1-301; Coverage: 100%)
Gene name: aph(2'')-Id
Sequence domains: Phosphotransferase enzyme family
Structure domains:

Ligands and Environments

3 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 43.141Å b: 101.814Å c: 70.249Å
α: 90° β: 96.86° γ: 90°
R R work R free
0.222 0.219 0.27
Expression system: Escherichia coli BL21(DE3)