1lox

<StructureSection load='1lox' size='340' side='right' caption='[[1lox]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[1lox]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LOX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1LOX FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=RS7:(2E)-3-(2-OCT-1-YN-1-YLPHENYL)ACRYLIC+ACID'>RS7</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Arachidonate_15-lipoxygenase Arachidonate 15-lipoxygenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.33 1.13.11.33] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lox OCA], [http://pdbe.org/1lox PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lox RCSB], [http://www.ebi.ac.uk/pdbsum/1lox PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lo/1lox_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.

The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.,Gillmor SA, Villasenor A, Fletterick R, Sigal E, Browner MF Nat Struct Biol. 1997 Dec;4(12):1003-9. PMID:9406550<ref>PMID:9406550</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1lox" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Arachidonate 15-lipoxygenase]]

[[Category: Browner, M F]]

[[Category: Fletterick, R J]]

[[Category: Gillmor, S A]]

[[Category: Sigal, E]]

[[Category: Villasenor, A]]

[[Category: Oxidoreductase]]