› 3o8y

X-ray diffraction
2.39Å resolution

Stable-5-Lipoxygenase

Released:
DOI: 10.2210/pdb3o8y/pdb
PDB 3o8y coloured by chain and viewed from the front.
PDB 3o8y coloured by chain and viewed from the side.
PDB 3o8y coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
The structure of human 5-lipoxygenase.
Gilbert NC, Bartlett SG, Waight MT, Neau DB, Boeglin WE, Brash AR, Newcomer ME
Science 331 217-9 (2011)
PMID: 21233389

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)
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: 79.44 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-E
Spacegroup: P21
Unit cell:
a: 55.17Å b: 202.89Å c: 76.8Å
α: 90° β: 109.56° γ: 90°
R-values:
R R work R free
0.182 0.182 0.21
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Dysregulation of Epigenetic Mechanisms of Gene Expression in the Pathologies of Hyperhomocysteinemia.
Perła-Kaján et al. (2019)
23 more

36 mentions without citation

Leukotriene biosynthetic enzymes as therapeutic targets.
Haeggström JZ. (2018)
35 more