3b7t: Difference between revisions

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-[[Image:3b7t.png|left|200px]]
-<!--
+==[E296Q]LTA4H in complex with Arg-Ala-Arg substrate==
-The line below this paragraph, containing "STRUCTURE_3b7t", creates the "Structure Box" on the page.
+<StructureSection load='3b7t' size='340' side='right'caption='[[3b7t]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3b7t]] is a 2 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=3B7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3B7T FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
-{{STRUCTURE_3b7t|  PDB=3b7t  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3b7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3b7t OCA], [https://pdbe.org/3b7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3b7t RCSB], [https://www.ebi.ac.uk/pdbsum/3b7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3b7t ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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/b7/3b7t_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/main_output.php?pdb_ID=3b7t ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+M1 aminopeptidases comprise a large family of biologically important zinc enzymes. We show that peptide turnover by the M1 prototype, leukotriene A4 hydrolase/aminopeptidase, involves a shift in substrate position associated with exchange of zinc coordinating groups, while maintaining the overall coordination geometry. The transition state is stabilized by residues conserved among M1 members and in the final reaction step, Glu-296 of the canonical zinc binding HEXXH motif shuffles a proton from the hydrolytic water to the leaving group. Tripeptide substrates bind along the conserved GXMEN motif, precisely occupying the distance between Glu-271 and Arg-563, whereas the Arg specificity is governed by a narrow S1 pocket capped with Asp-375. Our data provide detailed insights to the active site chemistry of M1 aminopeptidases and will aid in the development of novel enzyme inhibitors.
-===[E296Q]LTA4H in complex with Arg-Ala-Arg substrate===
+Structure-based dissection of the active site chemistry of leukotriene A4 hydrolase: implications for M1 aminopeptidases and inhibitor design.,Tholander F, Muroya A, Roques BP, Fournie-Zaluski MC, Thunnissen MM, Haeggstrom JZ Chem Biol. 2008 Sep 22;15(9):920-9. PMID:18804029<ref>PMID:18804029</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_18804029}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3b7t" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 18804029 is the PubMed ID number.
--->
-{{ABSTRACT_PUBMED_18804029}}
-==About this Structure==
-[[3b7t]] is a 2 chain structure of [[Leukotriene A4 Hydrolase]] 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=3B7T OCA].
 ==See Also==
-*[[Leukotriene A4 Hydrolase]]
+*[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]]
+== References ==
-==Reference==
+<references/>
-<ref group="xtra">PMID:18804029</ref><ref group="xtra">PMID:17357161</ref><ref group="xtra">PMID:15078870</ref><ref group="xtra">PMID:11675384</ref><ref group="xtra">PMID:11917124</ref><ref group="xtra">PMID:11175901</ref><references group="xtra"/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Fournie-Zaluski, M C.]]
+[[Category: Large Structures]]
-[[Category: Haeggstrom, J.]]
+[[Category: Fournie-Zaluski M-C]]
-[[Category: Muroya, A.]]
+[[Category: Haeggstrom J]]
-[[Category: Roques, B P.]]
+[[Category: Muroya A]]
-[[Category: Tholander, F.]]
+[[Category: Roques B-P]]
-[[Category: Thunnissen, M.]]
+[[Category: Tholander F]]
-[[Category: Alternative splicing]]
+[[Category: Thunnissen M]]
-[[Category: Analogue peptide]]
-[[Category: Cytoplasm]]
-[[Category: Hydrolase]]
-[[Category: Hydrolysis]]
-[[Category: Leukotriene biosynthesis]]
-[[Category: Metal-binding]]
-[[Category: Metalloprotease]]
-[[Category: Multifunctional enzyme]]
-[[Category: Protease]]
-[[Category: Transition state]]
-[[Category: Tripeptide substrate]]
-[[Category: Zinc]]