› 3pss

X-ray diffraction
2Å resolution

Crystal Structure of AhQnr, the Qnr protein from Aeromonas hydrophila (P21 crystal form)

Released:
DOI: 10.2210/pdb3pss/pdb
PDB entry 3pss coloured by chain, front view.
PDB entry 3pss coloured by chain, side view.
PDB entry 3pss coloured by chain, top view.
Source organism: Aeromonas hydrophila subsp. hydrophila ATCC 7966
Primary publication:
Structural insights into quinolone antibiotic resistance mediated by pentapeptide repeat proteins: conserved surface loops direct the activity of a Qnr protein from a gram-negative bacterium.
Xiong X, Bromley EH, Oelschlaeger P, Woolfson DN, Spencer J
Nucleic Acids Res 39 3917-27 (2011)
PMID: 21227918

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106094 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Qnr Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 24.33 KDa
Source organism: Aeromonas hydrophila subsp. hydrophila ATCC 7966
Expression system: Escherichia coli
UniProt:
  • Canonical: A0KF03 (Residues: 1-216; Coverage: 100%)
Gene name: AHA_0291
Sequence domains: Pentapeptide repeats (8 copies)
Structure domains: E3 ubiquitin-protein ligase SopA

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MLY 6 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 52.23Å b: 57.71Å c: 85.12Å
α: 90° β: 106.96° γ: 90°
R-values:
R R work R free
0.181 0.179 0.233
Expression system: Escherichia coli

Quick links

Citations

19 review citations

Mechanism of quinolone action and resistance.
Aldred et al. (2014)
18 more

6 mentions without citation

Mechanisms of drug resistance: quinolone resistance.
Hooper et al. (2015)
5 more