› 3rde

X-ray diffraction
1.89Å resolution

Crystal structure of the catalytic domain of porcine leukocyte 12-lipoxygenase

Released:
DOI: 10.2210/pdb3rde/pdb
PDB entry 3rde coloured by chain, front view.
PDB entry 3rde coloured by chain, side view.
PDB entry 3rde coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Crystal structure of 12-lipoxygenase catalytic-domain-inhibitor complex identifies a substrate-binding channel for catalysis.
Xu S, Mueser TC, Marnett LJ, Funk MO
Structure 20 1490-7 (2012)
PMID: 22795085

Function and Biology Details

Reactions catalysed: 
Alpha-linolenate + O(2) = (9Z,11E,13S,15Z)-13-hydroperoxyoctadeca-9,11,15-trienoate
Arachidonate + O(2) = (5Z,8Z,10E,14Z)-(12S)-12-hydroperoxyicosa-5,8,10,14-tetraenoate
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

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-147734 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyunsaturated fatty acid lipoxygenase ALOX15 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 573 amino acids
Theoretical weight: 64.77 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P16469 (Residues: 112-663; Coverage: 83%)
Gene name: ALOX15
Sequence domains: Lipoxygenase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand K 2 x K
Ligand FE2 4 x FE2
Ligand OYP 4 x OYP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P21
Unit cell:
a: 83.45Å b: 181.54Å c: 91.61Å
α: 90° β: 92.86° γ: 90°
R-values:
R R work R free
0.173 0.172 0.214
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Mammalian lipoxygenases and their biological relevance.
Kuhn et al. (2015)
12 more

18 mentions without citation

The structural basis for specificity in lipoxygenase catalysis.
Newcomer et al. (2015)
17 more