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==THE ACTIVE SITE OF ASPARTIC PROTEINASES== | ==THE ACTIVE SITE OF ASPARTIC PROTEINASES== | ||
<StructureSection load='1er8' size='340' side='right' caption='[[1er8]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1er8' size='340' side='right'caption='[[1er8]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1er8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crypa Crypa]. 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 [http:// | <table><tr><td colspan='2'>[[1er8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Crypa Crypa]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1ER8 FirstGlance]. <br> | ||
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DHI:D-HISTIDINE'>DHI</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DHI:D-HISTIDINE'>DHI</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EAPA, EPN-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5116 CRYPA])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EAPA, EPN-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=5116 CRYPA])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1er8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1er8 OCA], [http://pdbe.org/1er8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1er8 RCSB], [http://www.ebi.ac.uk/pdbsum/1er8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1er8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| Line 13: | Line 13: | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/1er8_consurf.spt"</scriptWhenChecked> | <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/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 28: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1er8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1er8" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Pepsin|Pepsin]] | |||
*[[Proteinase|Proteinase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 34: | Line 38: | ||
[[Category: Crypa]] | [[Category: Crypa]] | ||
[[Category: Endothiapepsin]] | [[Category: Endothiapepsin]] | ||
[[Category: Large Structures]] | |||
[[Category: Blundell, T L]] | [[Category: Blundell, T L]] | ||
[[Category: Cooper, J B]] | [[Category: Cooper, J B]] | ||
Revision as of 13:24, 18 November 2020
THE ACTIVE SITE OF ASPARTIC PROTEINASESTHE ACTIVE SITE OF ASPARTIC PROTEINASES
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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.,Pearl L, Blundell T FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:6381096[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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