1er8: Difference between revisions

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-{{Seed}}
-[[Image:1er8.png|left|200px]]
-<!--
+==THE ACTIVE SITE OF ASPARTIC PROTEINASES==
-The line below this paragraph, containing "STRUCTURE_1er8", creates the "Structure Box" on the page.
+<StructureSection load='1er8' size='340' side='right'caption='[[1er8]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1er8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica] and [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ER8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ER8 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DHI:D-HISTIDINE'>DHI</scene></td></tr>
-{{STRUCTURE_1er8|  PDB=1er8  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1er8 OCA], [https://pdbe.org/1er8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1er8 RCSB], [https://www.ebi.ac.uk/pdbsum/1er8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1er8 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CARP_CRYPA CARP_CRYPA]
+== 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/er/1er8_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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=1er8 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The active site of the aspartic proteinase, endothiapepsin, has been defined by X-ray analysis and restrained least-squares refinement at 2.1 A resolution with a crystallographic agreement value of 0.16. The environments of the two catalytically important aspartyl groups are remarkably similar and the contributions of the NH2- and COOH-terminal domains to the catalytic centre are related by a local 2-fold axis. The carboxylates of the aspartyls share a hydrogen bond and have equivalent contacts to a bound water molecule or hydroxonium ion lying on the local diad. The main chains around 32 and 215 are connected by a novel interaction involving diad-related threonines. It is suggested that the two pKa values of the active site aspartyls arise from a structure not unlike that in maleic acid with a hydrogen-bonded intermediate species and a dicarboxylate characterised by electrostatic repulsions between the two negatively charged groups.
-===THE ACTIVE SITE OF ASPARTIC PROTEINASES===
+The active site of aspartic proteinases.,Pearl L, Blundell T FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096<ref>PMID:6381096</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1er8" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_6381096}}, adds the Publication Abstract to the page
+*[[Pepsin|Pepsin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 6381096 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_6381096}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Cryphonectria parasitica]]
-ER8 is a 2 chains structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ER8 OCA].
+[[Category: Equus caballus]]
+[[Category: Large Structures]]
-==Reference==
+[[Category: Blundell TL]]
-<ref group="xtra">PMID:6381096</ref><references group="xtra"/>
+[[Category: Cooper JB]]
-[[Category: Hydrolase]]
+[[Category: Hemmings AM]]
-[[Category: Blundell, T L.]]
+[[Category: Szelke M]]
-[[Category: Cooper, J B.]]
+[[Category: Veerapandian B]]
-[[Category: Hemmings, A M.]]
-[[Category: Szelke, M.]]
-[[Category: Veerapandian, B.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 15:27:57 2009''