1f34: Difference between revisions

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 <StructureSection load='1f34' size='340' side='right'caption='[[1f34]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascsu Ascsu] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F34 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1f34]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F34 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F34 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f32|1f32]]</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=1f34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f34 OCA], [https://pdbe.org/1f34 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f34 RCSB], [https://www.ebi.ac.uk/pdbsum/1f34 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f34 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f34 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f34 OCA], [http://pdbe.org/1f34 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f34 RCSB], [http://www.ebi.ac.uk/pdbsum/1f34 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f34 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG]] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent. [[http://www.uniprot.org/uniprot/API3_ASCSU API3_ASCSU]] This is an inhibitor of the aspartic protease pepsin.
+[https://www.uniprot.org/uniprot/PEPA_PIG PEPA_PIG] Shows particularly broad specificity; although bonds involving phenylalanine and leucine are preferred, many others are also cleaved to some extent.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 </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=1f34 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The three-dimensional structures of pepsin inhibitor-3 (PI-3) from Ascaris suum and of the complex between PI-3 and porcine pepsin at 1. 75 A and 2.45 A resolution, respectively, have revealed the mechanism of aspartic protease inhibition by this unique inhibitor. PI-3 has a new fold consisting of two domains, each comprising an antiparallel beta-sheet flanked by an alpha-helix. In the enzyme-inhibitor complex, the N-terminal beta-strand of PI-3 pairs with one strand of the 'active site flap' (residues 70-82) of pepsin, thus forming an eight-stranded beta-sheet that spans the two proteins. PI-3 has a novel mode of inhibition, using its N-terminal residues to occupy and therefore block the first three binding pockets in pepsin for substrate residues C-terminal to the scissile bond (S1'-S3'). The molecular structure of the pepsin-PI-3 complex suggests new avenues for the rational design of proteinaceous aspartic proteinase inhibitors.
-Structural basis for the inhibition of porcine pepsin by Ascaris pepsin inhibitor-3.,Ng KK, Petersen JF, Cherney MM, Garen C, Zalatoris JJ, Rao-Naik C, Dunn BM, Martzen MR, Peanasky RJ, James MN Nat Struct Biol. 2000 Aug;7(8):653-7. PMID:10932249<ref>PMID:10932249</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1f34" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Pepsin|Pepsin]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Ascsu]]
+[[Category: Ascaris suum]]
 [[Category: Large Structures]]
-[[Category: Pepsin A]]
 [[Category: Sus scrofa]]
-[[Category: Cherney, M M]]
+[[Category: Cherney MM]]
-[[Category: Garen, C]]
+[[Category: Garen C]]
-[[Category: James, M N]]
+[[Category: James MN]]
-[[Category: Ng, K K]]
+[[Category: Ng KK]]
-[[Category: Petersen, J F]]
+[[Category: Petersen JF]]
-[[Category: Hydrolase-hydrolase inhibitor complex]]
-[[Category: Proteinase-inhibitor complex]]