› 4dta

X-ray diffraction
2.35Å resolution

Crystal Structure of F95M Aminoglycoside-2''-Phosphotransferase Type IVa in Complex with Adenosine

Released:
DOI: 10.2210/pdb4dta/pdb
PDB entry 4dta coloured by chain, front view.
PDB entry 4dta coloured by chain, side view.
PDB entry 4dta coloured by chain, top view.
Source organism: Enterococcus casseliflavus
Primary publication:
Structural basis for dual nucleotide selectivity of aminoglycoside 2''-phosphotransferase IVa provides insight on determinants of nucleotide specificity of aminoglycoside kinases.
Shi K, Berghuis AM
J Biol Chem 287 13094-102 (2012)
PMID: 22371504

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-130603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoglycoside phosphotransferase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 309 amino acids
Theoretical weight: 36.48 KDa
Source organism: Enterococcus casseliflavus
Expression system: Escherichia coli
UniProt:
  • Canonical: O68183 (Residues: 1-301; Coverage: 100%)
Gene name: aph(2'')-Id
Sequence domains: Phosphotransferase enzyme family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADN 2 x ADN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 42.113Å b: 101.055Å c: 73.031Å
α: 90° β: 99.94° γ: 90°
R-values:
R R work R free
0.201 0.198 0.257
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Role of protein kinase CK2 in antitumor drug resistance.
Borgo et al. (2019)
3 more

3 mentions without citation

Strategies to overcome the action of aminoglycoside-modifying enzymes for treating resistant bacterial infections.
Labby et al. (2013)
2 more