› 1lox

X-ray diffraction
2.4Å resolution

RABBIT RETICULOCYTE 15-LIPOXYGENASE

Released:
DOI: 10.2210/pdb1lox/pdb
PDB entry 1lox coloured by chain, front view.
PDB entry 1lox coloured by chain, side view.
PDB entry 1lox coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.
Gillmor SA, Villaseñor A, Fletterick R, Sigal E, Browner MF
Nat Struct Biol 4 1003-9 (1997)
PMID: 9406550

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyunsaturated fatty acid lipoxygenase ALOX15 Chain: A
Molecule details ›
Chain: A
Length: 662 amino acids
Theoretical weight: 75.25 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P12530 (Residues: 2-663; Coverage: 100%)
Gene name: ALOX15
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand FE2 1 x FE2
Ligand RS7 1 x RS7
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: R32
Unit cell:
a: 198.9Å b: 198.9Å c: 136.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.198 0.247

Quick links

Citations

50 review citations

The lipoxygenase pathway.
Feussner et al. (2002)
49 more

39 mentions without citation

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