3d3l

X-ray diffraction
2.6Å resolution

The 2.6 A crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12S-type

Released:
Source organism: Homo sapiens
Entry authors: Tresaugues L, Moche M, Arrowsmith CH, Berglund H, Busam RD, Collins R, Dahlgren LG, Edwards AM, Flodin S, Flores A, Graslund S, Hammarstrom M, Herman MD, Johansson A, Johansson I, Kallas A, Karlberg T, Kotenyova T, Lehtio L, Nilsson ME, Nyman T, Olesen K, Persson C, Sagemark J, Schueler H, Svensson L, Thorsell AG, Van Den Berg S, Welin M, Weigelt J, Wikstrom M, Nordlund P, Structural Genomics Consortium (SGC)

Function and Biology Details

Reactions catalysed:
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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-148273 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyunsaturated fatty acid lipoxygenase ALOX12 Chains: A, B
Molecule details ›
Chains: A, B
Length: 541 amino acids
Theoretical weight: 61.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P18054 (Residues: 172-663; Coverage: 74%)
Gene names: 12LO, ALOX12, LOG12
Sequence domains: Lipoxygenase
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P1
Unit cell:
a: 59.59Å b: 70.153Å c: 77.868Å
α: 65.37° β: 88.01° γ: 69.82°
R-values:
R R work R free
0.21 0.206 0.276
Expression system: Escherichia coli