PDB ID or protein name

2p0m » Arachidonate 15-lipoxygenase

2p0m » Arachidonate 15-lipoxygenase
Magnify 2p0m » Arachidonate 15-lipoxygenaseEnlarged view of image
3D view in Jmol or Webmol

gray dot

Download Coordinates

gray dot

Topology in Eukaryotic plasma membrane
Topologyextracellular side
cytoplasmic side
2p0m » Arachidonate 15-lipoxygenase
Depth 8.6 ± 0.1 Å
Tilt Angle 87 ± 5°
ΔGtransfer -14.3 kcal/mol
Links to 2p0m PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 2.4 Å
Other PDB entries representing this structure 1lox
Number of subunits 1
Experimental Verification for 2p0m » Arachidonate 15-lipoxygenase
Results are consistent with the membrane-anchoring role of Y15, F70, L71, W181 and L195 (Walther et al. 2004). The following residues are buried in the membrane in the calculated position of the protein: L71, I194, L195, L291, Y292, and F412 (Y15 and F70 are close to the calculated hydrophobic boundary, and W181 is missing in the crystal structure). Membrane binding affinity is -4.6 kcal/mol (Walther et al. 2004).
1 reference
Walter M, Wiener R, and Kuhn H. 2004. Investigations into calcium-dependent membrane association of 15-lipoxygenase-1. J. Biol. Chem., 279: 3717-3725. PubMed
Comments on 2p0m » Arachidonate 15-lipoxygenase
Alpha-helical lipoxygenases, alpha-helical phospholipase C, and alpha/beta pancreatic lipases have a common C2 domain.