3er3: Difference between revisions

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{{Seed}}
[[Image:3er3.png|left|200px]]


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==The active site of aspartic proteinases==
The line below this paragraph, containing "STRUCTURE_3er3", creates the "Structure Box" on the page.
<StructureSection load='3er3' size='340' side='right'caption='[[3er3]], [[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'>[[3er3]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3ER3 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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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></td></tr>
{{STRUCTURE_3er3|  PDB=3er3  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3er3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3er3 OCA], [https://pdbe.org/3er3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3er3 RCSB], [https://www.ebi.ac.uk/pdbsum/3er3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3er3 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/3er3_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=3er3 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 3er3" style="background-color:#fffaf0;"></div>


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==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]]
3ER3 is a 2 chains structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ER3 OCA].
[[Category: Large Structures]]
 
[[Category: Al-Karadaghi S]]
==Reference==
[[Category: Blundell TL]]
<ref group="xtra">PMID:6381096</ref><references group="xtra"/>
[[Category: Cooper JB]]
[[Category: Hydrolase]]
[[Category: Hoover D]]
[[Category: Al-Karadaghi, S.]]
[[Category: Veerapandian B]]
[[Category: Blundell, T L.]]
[[Category: Cooper, J B.]]
[[Category: Hoover, D.]]
[[Category: Veerapandian, B.]]
 
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Retrieved from "https://proteopedia.org/3er3"