1egp: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 ==PROTEINASE INHIBITOR EGLIN C WITH HYDROLYSED REACTIVE CENTER==
-<StructureSection load='1egp' size='340' side='right' caption='[[1egp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1egp' size='340' side='right'caption='[[1egp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1egp]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1EGP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1egp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hirudo_medicinalis Hirudo medicinalis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGP FirstGlance]. <br>
-</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=1egp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egp OCA], [http://pdbe.org/1egp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1egp RCSB], [http://www.ebi.ac.uk/pdbsum/1egp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1egp ProSAT]</span></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&#8491;</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=1egp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egp OCA], [https://pdbe.org/1egp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egp RCSB], [https://www.ebi.ac.uk/pdbsum/1egp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME]] Inhibits both elastase and cathepsin G.
+[https://www.uniprot.org/uniprot/ICIC_HIRME ICIC_HIRME] Inhibits both elastase and cathepsin G.
 == 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/eg/1egp_consurf.spt"</scriptWhenChecked>
+     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/eg/1egp_consurf.spt"</scriptWhenChecked>
      <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 18: / Line 19: @@
 </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=1egp ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The inhibition of serine proteinases by both synthetic and natural inhibitors has been widely studied. Eglin c is a small thermostable protein isolated from the leech, Hirudo medicinalis. Eglin c is a potent serine proteinase inhibitor. The three-dimensional structure of native eglin and of its complexes with a number of proteinases are known. We here describe the crystal structure of hydrolysed eglin not bound to a proteinase. The body of the eglin has a conformation remarkably similar to that in the known complexes with proteinases. However, the peptide chain has been cut at the 'scissile' bond between residues 45 and 46, presumed to result from the presence of subtilisin DY in the crystallisation sample. The residues usually making up the inhibiting loop of eglin take up a quite different conformation in the nicked inhibitor leading to stabilising contacts between neighbouring molecules in the crystal. The structure was solved by molecular replacement techniques and refined to a final R-factor of 14.5%.
-Structure of the proteinase inhibitor eglin c with hydrolysed reactive centre at 2.0 A resolution.,Betzel C, Dauter Z, Genov N, Lamzin V, Navaza J, Schnebli HP, Visanji M, Wilson KS FEBS Lett. 1993 Feb 15;317(3):185-8. PMID:8425603<ref>PMID:8425603</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1egp" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Eglin|Eglin]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
 [[Category: Hirudo medicinalis]]
-[[Category: Betzel, C]]
+[[Category: Large Structures]]
-[[Category: Dauter, Z]]
+[[Category: Betzel C]]
-[[Category: Lamzin, V]]
+[[Category: Dauter Z]]
-[[Category: Wilson, K S]]
+[[Category: Lamzin V]]
-[[Category: Proteinase inhibitor]]
+[[Category: Wilson KS]]