View source for 4lp9


==Endothiapepsin complexed with Phe-reduced-Tyr peptide.==
<StructureSection load='4lp9' size='340' side='right'caption='[[4lp9]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4lp9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LP9 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]] 1.35&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=22G:N-[(2S)-2-AMINO-3-PHENYLPROPYL]-L-TYROSINE'>22G</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4lp9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lp9 OCA], [https://pdbe.org/4lp9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lp9 RCSB], [https://www.ebi.ac.uk/pdbsum/4lp9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lp9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CARP_CRYPA CARP_CRYPA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endothiapepsin is a typical member of the aspartic proteinase family. The catalytic mechanism of this family is attributed to two conserved catalytic aspartate residues, which coordinate the hydrolysis of a peptide bond. An oligopeptide inhibitor (IC50 = 0.62 microM) based on a reduced-bond transition-state inhibitor of mucorpepsin was co-crystallized with endothiapepsin and the crystal structure of the enzyme-inhibitor complex was determined at 1.35 A resolution. A total of 12 hydrogen bonds between the inhibitor and the active-site residues were identified. The resulting structure demonstrates a number of novel subsite interactions in the active-site cleft.

The structure of endothiapepsin complexed with a Phe-Tyr reduced-bond inhibitor at 1.35 A resolution.,Guo J, Cooper JB, Wood SP Acta Crystallogr F Struct Biol Commun. 2014 Jan;70(Pt 1):30-3. doi:, 10.1107/S2053230X13032974. Epub 2013 Dec 24. PMID:24419612<ref>PMID:24419612</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4lp9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cryphonectria parasitica]]
[[Category: Large Structures]]
[[Category: Cooper JB]]
[[Category: Guo J]]
[[Category: Wood SP]]