3chs: Difference between revisions

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 ==Crystal structure of leukotriene A4 hydrolase in complex with (2S)-2-amino-5-[[4-[(2S)-2-hydroxy-2-phenyl-ethoxy]phenyl]amino]-5-oxo-pentanoic acid==
-<StructureSection load='3chs' size='340' side='right' caption='[[3chs]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
+<StructureSection load='3chs' size='340' side='right'caption='[[3chs]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3chs]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CHS FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3chs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHS FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4BU:(2S)-2-AMINO-5-[[4-[(2S)-2-HYDROXY-2-PHENYL-ETHOXY]PHENYL]AMINO]-5-OXO-PENTANOIC+ACID'>4BU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.55&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1hs6|1hs6]], [[1gw6|1gw6]], [[1h19|1h19]], [[1sqm|1sqm]], [[3cho|3cho]], [[3chp|3chp]], [[3chq|3chq]], [[3chr|3chr]], [[2vj8|2vj8]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4BU:(2S)-2-AMINO-5-[[4-[(2S)-2-HYDROXY-2-PHENYL-ETHOXY]PHENYL]AMINO]-5-OXO-PENTANOIC+ACID'>4BU</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=YB:YTTERBIUM+(III)+ION'>YB</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LTA4H, LTA4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chs OCA], [https://pdbe.org/3chs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chs RCSB], [https://www.ebi.ac.uk/pdbsum/3chs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chs ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leukotriene-A(4)_hydrolase Leukotriene-A(4) hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.2.6 3.3.2.6] </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=3chs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3chs RCSB], [http://www.ebi.ac.uk/pdbsum/3chs PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LKHA4_HUMAN LKHA4_HUMAN]] Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.<ref>PMID:1897988</ref> <ref>PMID:1975494</ref> <ref>PMID:2244921</ref> <ref>PMID:12207002</ref> <ref>PMID:11917124</ref> <ref>PMID:15078870</ref> <ref>PMID:18804029</ref>
+[https://www.uniprot.org/uniprot/LKHA4_HUMAN LKHA4_HUMAN] Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity.<ref>PMID:1897988</ref> <ref>PMID:1975494</ref> <ref>PMID:2244921</ref> <ref>PMID:12207002</ref> <ref>PMID:11917124</ref> <ref>PMID:15078870</ref> <ref>PMID:18804029</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
    <jmolCheckbox>
-     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chs_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chs_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
-</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].
+</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/main_output.php?pdb_ID=3chs ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Leukotriene B(4) (LTB(4)) is a potent pro-inflammatory mediator that has been implicated in the pathogenesis of multiple diseases, including psoriasis, inflammatory bowel disease, multiple sclerosis and asthma. As a method to decrease the level of LTB(4) and possibly identify novel treatments, inhibitors of the LTB(4) biosynthetic enzyme, leukotriene A(4) hydrolase (LTA(4)-h), have been explored. Here we describe the discovery of a potent inhibitor of LTA(4)-h, arylamide of glutamic acid 4f, starting from the corresponding glycinamide 2. Analogs of 4f are then described, focusing on compounds that are both active and stable in whole blood. This effort culminated in the identification of amino alcohol 12a and amino ester 6b which meet these criteria.
-Synthesis of glutamic acid analogs as potent inhibitors of leukotriene A4 hydrolase.,Kirkland TA, Adler M, Bauman JG, Chen M, Haeggstrom JZ, King B, Kochanny MJ, Liang AM, Mendoza L, Phillips GB, Thunnissen M, Trinh L, Whitlow M, Ye B, Ye H, Parkinson J, Guilford WJ Bioorg Med Chem. 2008 May 1;16(9):4963-83. Epub 2008 Mar 20. PMID:18394906<ref>PMID:18394906</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
 ==See Also==
@@ Line 37: / Line 28: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Adler, M]]
+[[Category: Large Structures]]
-[[Category: Thunnissen, M M.G M]]
+[[Category: Adler M]]
-[[Category: Whitlow, M]]
+[[Category: Thunnissen MMGM]]
-[[Category: Alpha-beta protein]]
+[[Category: Whitlow M]]
-[[Category: Epoxide hydrolase]]
-[[Category: Hydrolase]]
-[[Category: Inhibitor complex]]
-[[Category: Leukotriene biosynthesis]]
-[[Category: Metal-binding]]
-[[Category: Metalloprotease]]
-[[Category: Multifunctional enzyme]]