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[[Image:3er3.png|left|200px]]
==The active site of aspartic proteinases==
<StructureSection load='3er3' size='340' side='right' caption='[[3er3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3er3]] is a 1 chain structure with sequence 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=3ER3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ER3 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0EL:6-AMMONIO-N-[(2R,4R,5R)-5-{[N-(TERT-BUTOXYCARBONYL)-L-PHENYLALANYL-3-(1H-IMIDAZOL-3-IUM-4-YL)-L-ALANYL]AMINO}-6-CYCLOHEXYL-4-HYDROXY-2-(2-METHYLPROPYL)HEXANOYL]-L-NORLEUCYLPHENYLALANINE'>0EL</scene><br>
<tr><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>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3er3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3er3 RCSB], [http://www.ebi.ac.uk/pdbsum/3er3 PDBsum]</span></td></tr>
<table>
== 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/3er3_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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/chain_selection.php?pdb_ID=2ata 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.


{{STRUCTURE_3er3|  PDB=3er3  |  SCENE=  }}
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>


===The active site of aspartic proteinases===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_6381096}}
 
==About this Structure==
[[3er3]] is a 1 chain structure with sequence 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=3ER3 OCA].


==See Also==
==See Also==
*[[Pepsin|Pepsin]]
*[[Pepsin|Pepsin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:006381096</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Cryphonectria parasitica]]
[[Category: Cryphonectria parasitica]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
Retrieved from "https://proteopedia.org/3er3"