› 3o8y

X-ray diffraction
2.39Å resolution

Stable-5-Lipoxygenase

Released:
DOI: 10.2210/pdb3o8y/pdb
PDB entry 3o8y coloured by chain, front view.
PDB entry 3o8y coloured by chain, side view.
PDB entry 3o8y coloured by chain, top view.
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)
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: 79.44 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

31 review citations

Lipoxygenase and leukotriene pathways: biochemistry, biology, and roles in disease.
Haeggström et al. (2011)
30 more

67 mentions without citation

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