4lp9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Endothiapepsin complexed with Phe-reduced-Tyr peptide.== | |
| + | <StructureSection load='4lp9' size='340' side='right'caption='[[4lp9]], [[Resolution|resolution]] 1.35Å' 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]] 1.35Å</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®/PubMed®, 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]] | ||
Current revision
Endothiapepsin complexed with Phe-reduced-Tyr peptide.
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