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3d3l
From Proteopedia
(Difference between revisions)
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| - | ==The 2.6 A crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12S-type | + | ==The 2.6 A crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12S-type== |
| - | <StructureSection load='3d3l' size='340' side='right' caption='[[3d3l]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='3d3l' size='340' side='right'caption='[[3d3l]], [[Resolution|resolution]] 2.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3d3l]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3d3l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3D3L FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALOX12, LOG12 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ALOX12, LOG12 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Arachidonate_12-lipoxygenase Arachidonate 12-lipoxygenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.31 1.13.11.31] </span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3d3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3d3l OCA], [https://pdbe.org/3d3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3d3l RCSB], [https://www.ebi.ac.uk/pdbsum/3d3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3d3l ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/LOX12_HUMAN LOX12_HUMAN]] Oxygenase and 14,15-leukotriene A4 synthase activity. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Arachidonate 12-lipoxygenase]] | [[Category: Arachidonate 12-lipoxygenase]] | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Arrowsmith, C H]] | [[Category: Arrowsmith, C H]] | ||
[[Category: Berg, S Van Den]] | [[Category: Berg, S Van Den]] | ||
Revision as of 19:18, 20 October 2021
The 2.6 A crystal structure of the lipoxygenase domain of human arachidonate 12-lipoxygenase, 12S-type
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Categories: Arachidonate 12-lipoxygenase | Human | Large Structures | Arrowsmith, C H | Berg, S Van Den | Berglund, H | Busam, R D | Collins, R | Dahlgren, L G | Edwards, A M | Flodin, S | Flores, A | Graslund, S | Hammarstrom, M | Herman, M D | Johansson, A | Johansson, I | Kallas, A | Karlberg, T | Kotenyova, T | Lehtio, L | Moche, M | Nilsson, M E | Nordlund, P | Nyman, T | Olesen, K | Persson, C | Structural genomic | Sagemark, J | Schueler, H | Svensson, L | Thorsell, A G | Tresaugues, L | Weigelt, J | Welin, M | Wikstrom, M | 12-lox | Alox12 | Arachidonate | Cytoplasm | Dioxygenase | Iron-binding protein | Leukotriene biosynthesis | Metal-binding | Oxidoreductase | Oxygenase | Platelet-type lipoxygenase 12 | Polymorphism | Sgc
