› 1kny

X-ray diffraction
2.5Å resolution

KANAMYCIN NUCLEOTIDYLTRANSFERASE

Released:
DOI: 10.2210/pdb1kny/pdb
PDB entry 1kny coloured by chain, front view.
PDB entry 1kny coloured by chain, side view.
PDB entry 1kny coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase.
Pedersen LC, Benning MM, Holden HM
Biochemistry 34 13305-11 (1995)
PMID: 7577914

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138345 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Kanamycin nucleotidyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 253 amino acids
Theoretical weight: 28.87 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: P05057 (Residues: 1-253; Coverage: 100%)
Gene names: kan, knt
Sequence domains: KNTase C-terminal domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand APC 2 x APC
Ligand KAN 2 x KAN
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 57.3Å b: 102.2Å c: 108.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.168 not available
Expression system: Escherichia coli

Quick links

Citations

21 review citations

Aminoglycosides: activity and resistance.
Mingeot-Leclercq et al. (1999)
20 more

20 mentions without citation

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