› 5ir4

X-ray diffraction
1.48Å resolution

Crystal structure of wild-type bacterial lipoxygenase from Pseudomonas aeruginosa PA-LOX with space group C2221 at 1.48 A resolution

Released:
DOI: 10.2210/pdb5ir4/pdb
PDB entry 5ir4 coloured by chain, front view.
PDB entry 5ir4 coloured by chain, side view.
PDB entry 5ir4 coloured by chain, top view.
Source organism: Pseudomonas aeruginosa
Primary publication:
Structural and functional basis of phospholipid oxygenase activity of bacterial lipoxygenase from Pseudomonas aeruginosa.
Banthiya S, Kalms J, Galemou Yoga E, Ivanov I, Carpena X, Hamberg M, Kuhn H, Scheerer P
Biochim Biophys Acta 1861 1681-1692 (2016)
PMID: 27500637

Function and Biology Details

Reaction catalysed: 
Arachidonate + O(2) = (5Z,8Z,11Z,13E)-(15S)-15-hydroperoxyicosa-5,8,11,13-tetraenoate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipoxygenase LoxA Chain: A
Molecule details ›
Chain: A
Length: 688 amino acids
Theoretical weight: 75.05 KDa
Source organism: Pseudomonas aeruginosa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I4G8 (Residues: 9-685; Coverage: 100%)
Gene names: PA1169, loxA
Sequence domains: Lipoxygenase

Ligands and Environments

6 bound ligands:
Ligand FE2 1 x FE2
Ligand ZPE 1 x ZPE
Ligand GOL 7 x GOL
Ligand CL 1 x CL
Ligand MG 1 x MG
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2221
Unit cell:
a: 83.744Å b: 97.391Å c: 153.839Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.136 0.155
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Regulation of lipid peroxidation and ferroptosis in diverse species.
Conrad et al. (2018)
3 more

3 mentions without citation

A Comprehensive Review on Cannabis sativa Ethnobotany, Phytochemistry, Molecular Docking and Biological Activities.
Hourfane et al. (2023)
2 more