View source for 5fwq


==Apo structure of human Leukotriene A4 hydrolase==
<StructureSection load='5fwq' size='340' side='right'caption='[[5fwq]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5fwq]] 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=5FWQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FWQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.047&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fwq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fwq OCA], [https://pdbe.org/5fwq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fwq RCSB], [https://www.ebi.ac.uk/pdbsum/5fwq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fwq 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> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The leukotriene A4 hydrolase (LTA4H) is a bifunctional enzyme, containing a peptidase and a hydrolase activity both activities having opposing functions regulating inflammatory response. The hydrolase activity is responsible for the conversion of leukotriene A4 to pro-inflammatory leukotriene B4, and hence, selective inhibitors of the hydrolase activity are of high pharmacological interest. Here we present the thermodynamic characterization of structurally distinct inhibitors of the LTA4H that occupy different regions of the binding site using different biophysical methods. An in silico method for the determination of stabilized water molecules in the binding site of the apo structure of LTA4H is used to interpret the measured thermodynamic data and provided insights for design of novel LTA4H inhibitors.

Thermodynamic properties of leukotriene A4 hydrolase inhibitors.,Wittmann SK, Kalinowsky L, Kramer JS, Bloecher R, Knapp S, Steinhilber D, Pogoryelov D, Proschak E, Heering J Bioorg Med Chem. 2016 Aug 26. pii: S0968-0896(16)30655-1. doi:, 10.1016/j.bmc.2016.08.047. PMID:27651294<ref>PMID:27651294</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5fwq" style="background-color:#fffaf0;"></div>

==See Also==
*[[Leukotriene A4 Hydrolase|Leukotriene A4 Hydrolase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Bloecher R]]
[[Category: Heering J]]
[[Category: Kalinowsky L]]
[[Category: Kramer J]]
[[Category: Pogoryelov D]]
[[Category: Proschak E]]
[[Category: Steinhilber D]]
[[Category: Wittmann SK]]