› 3w0n

X-ray diffraction
1.9Å resolution

Crystal structure of a thermostable mutant of aminoglycoside phosphotransferase APH(4)-Ia, ternary complex with AMP-PNP and hygromycin B

Released:
DOI: 10.2210/pdb3w0n/pdb
PDB entry 3w0n coloured by chain, front view.
PDB entry 3w0n coloured by chain, side view.
PDB entry 3w0n coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structures of the ternary complex of APH(4)-Ia/Hph with hygromycin B and an ATP analog using a thermostable mutant.
Iino D, Takakura Y, Fukano K, Sasaki Y, Hoshino T, Ohsawa K, Nakamura A, Yajima S
J Struct Biol 183 76-85 (2013)
PMID: 23747390

Function and Biology Details

Reaction catalysed: 
ATP + hygromycin B = ADP + 4-O-phosphohygromycin B
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132716 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hygromycin-B 4-O-kinase Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 39.08 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P00557 (Residues: 1-341; Coverage: 100%)
Gene name: hph
Sequence domains: Phosphotransferase enzyme family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ANP 1 x ANP
Ligand HY0 1 x HY0
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P3221
Unit cell:
a: 70.348Å b: 70.348Å c: 124.073Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.176 0.199
Expression system: Escherichia coli

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Citations

1 review citation

Comprehensive review of chemical strategies for the preparation of new aminoglycosides and their biological activities.
Thamban Chandrika et al. (2018)
8 other articles

2 mentions without citation

Overcoming Aminoglycoside Enzymatic Resistance: Design of Novel Antibiotics and Inhibitors.
Zárate et al. (2018)
1 more