› 2p0m

X-ray diffraction
2.4Å resolution

Revised structure of rabbit reticulocyte 15S-lipoxygenase

Released:
DOI: 10.2210/pdb2p0m/pdb
PDB entry 2p0m coloured by chain, front view.
PDB entry 2p0m coloured by chain, side view.
PDB entry 2p0m coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Conformational flexibility in mammalian 15S-lipoxygenase: Reinterpretation of the crystallographic data.
Choi J, Chon JK, Kim S, Shin W
Proteins 70 1023-32 (2008)
PMID: 17847087

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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-146259 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyunsaturated fatty acid lipoxygenase ALOX15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 662 amino acids
Theoretical weight: 75.26 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 2 x FE2
Ligand RS7 1 x RS7
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R3
Unit cell:
a: 198.9Å b: 198.9Å c: 136.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.193 0.193 0.23

Quick links

Citations

9 review citations

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

28 mentions without citation

Structural and functional biology of arachidonic acid 15-lipoxygenase-1 (ALOX15).
Ivanov et al. (2015)
27 more