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4er1

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{{Seed}}
 
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[[Image:4er1.png|left|200px]]
 
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<!--
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==THE ACTIVE SITE OF ASPARTIC PROTEINASES==
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The line below this paragraph, containing "STRUCTURE_4er1", creates the "Structure Box" on the page.
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<StructureSection load='4er1' size='340' side='right'caption='[[4er1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[4er1]] is a 1 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=4ER1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ER1 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0ZP:N-[(1R,2R,4R)-1-(CYCLOHEXYLMETHYL)-2-HYDROXY-6-METHYL-4-{[(2R)-2-METHYLBUTYL]CARBAMOYL}HEPTYL]-3-(1H-IMIDAZOL-3-IUM-4-YL)-N~2~-[3-NAPHTHALEN-1-YL-2-(NAPHTHALEN-1-YLMETHYL)PROPANOYL]-L-ALANINAMIDE'>0ZP</scene></td></tr>
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-->
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.19, 3.4.23.20, 3.4.23.21, 3.4.23.22, 3.4.23.23, 3.4.23.24, 3.4.23.25, 3.4.23.26, 3.4.23.28 and 3.4.23.30] </span></td></tr>
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{{STRUCTURE_4er1| PDB=4er1 | SCENE= }}
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<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=4er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er1 OCA], [http://pdbe.org/4er1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4er1 RCSB], [http://www.ebi.ac.uk/pdbsum/4er1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4er1 ProSAT]</span></td></tr>
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</table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/4er1_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=4er1 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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===THE ACTIVE SITE OF ASPARTIC PROTEINASES===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4er1" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_6381096}}, adds the Publication Abstract to the page
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*[[Pepsin|Pepsin]]
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(as it appears on PubMed at http://www.pubmed.gov), where 6381096 is the PubMed ID number.
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== References ==
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-->
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<references/>
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{{ABSTRACT_PUBMED_6381096}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Crypa]]
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4ER1 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER1 OCA].
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==Reference==
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<ref group="xtra">PMID:6381096</ref><references group="xtra"/>
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[[Category: Cryphonectria parasitica]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
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[[Category: Blundell, T L.]]
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[[Category: Large Structures]]
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[[Category: Cooper, J B.]]
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[[Category: Blundell, T L]]
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[[Category: Quail, J W.]]
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[[Category: Cooper, J B]]
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[[Category: Szelke, M.]]
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[[Category: Quail, J W]]
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[[Category: Szelke, M]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 21:02:51 2009''
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[[Category: Acid proteinase]]
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[[Category: Hydrolase-hydrolase inhibitor complex]]

Current revision

THE ACTIVE SITE OF ASPARTIC PROTEINASES

PDB ID 4er1

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