› 6ctz

X-ray diffraction
1.34Å resolution

Structure of the GDP and kanamycin complex of APH(2")-IIia

Released:
DOI: 10.2210/pdb6ctz/pdb
PDB entry 6ctz coloured by chain, front view.
PDB entry 6ctz coloured by chain, side view.
PDB entry 6ctz coloured by chain, top view.
Source organism: Enterococcus gallinarum
Primary publication:
Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2''-phosphotransferases
Smith CA, Toth M, Stewart NK, Maltz L, Vakulenko SB
Acta Crystallogr. D Biol. Crystallogr. 75 1129-1137 (2019)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161249 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aminoglycoside phosphotransferase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 297 amino acids
Theoretical weight: 33.77 KDa
Source organism: Enterococcus gallinarum
Expression system: Escherichia coli
UniProt:
  • Canonical: P96762 (Residues: 5-301; Coverage: 97%)
Sequence domains: Phosphotransferase enzyme family
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand GDP 1 x GDP
Ligand MG 2 x MG
Ligand KAN 1 x KAN
Ligand CL 2 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21212
Unit cell:
a: 77.169Å b: 58.982Å c: 70.853Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.147 0.146 0.171
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Enterococcus Virulence and Resistant Traits Associated with Its Permanence in the Hospital Environment.
Geraldes et al. (2022)

1 mention without citation

Structural basis for the diversity of the mechanism of nucleotide hydrolysis by the aminoglycoside-2''-phosphotransferases.
Smith et al. (2019)