› 3v98

X-ray diffraction
2.07Å resolution

Function and Biology Details

Reaction catalysed: 
(1a) arachidonate + O(2) = (5S,6E,8Z,11Z,14Z)-5-hydroperoxyicosa-6,8,11,14-tetraenoate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyunsaturated fatty acid 5-lipoxygenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 691 amino acids
Theoretical weight: 79.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P09917 (Residues: 1-674; Coverage: 100%)
Gene names: ALOX5, LOG5
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand FE2 2 x FE2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 55.41Å b: 202.503Å c: 76.971Å
α: 90° β: 109.82° γ: 90°
R-values:
R R work R free
0.167 0.166 0.197
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

12 mentions without citation

Conversion of human 5-lipoxygenase to a 15-lipoxygenase by a point mutation to mimic phosphorylation at Serine-663.
Gilbert et al. (2012)
11 more