3chs: Difference between revisions

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[[Image:3chs.png|left|200px]]


{{STRUCTURE_3chs|  PDB=3chs  |  SCENE=  }}
==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=''>
===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===
== Structural highlights ==
 
<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>
{{ABSTRACT_PUBMED_18394906}}
</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='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>
==About this Structure==
<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>
[[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].  
</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/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/main_output.php?pdb_ID=3chs ConSurf].
<div style="clear:both"></div>


==See Also==
==See Also==
*[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]]
*[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:018394906</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[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]]

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