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New page: left|200px<br /> <applet load="1od1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1od1, resolution 1.37Å" /> '''ENDOTHIAPEPSIN PD13...
 
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[[Image:1od1.gif|left|200px]]<br />
<applet load="1od1" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1od1, resolution 1.37&Aring;" />
'''ENDOTHIAPEPSIN PD135,040 COMPLEX'''<br />


==Overview==
==Endothiapepsin PD135,040 complex==
The crystal structure of endothiapepsin complexed with the gem-diol, inhibitor PD-135,040 has been anisotropically refined to a resolution of, 1.37 A. The structure of this inhibitor complex is in agreement with, previous structures of endothiapepsin gem-diol inhibitor complexes that, have been used to develop proposed catalytic mechanisms. However, the, increase in resolution over previous structures confirms the presence of a, number of short hydrogen bonds within the active site that are likely to, play an important role in the catalytic mechanism. The presence of, low-barrier hydrogen bonds was indicated in a previous one-dimensional H, NMR spectrum.
<StructureSection load='1od1' size='340' side='right'caption='[[1od1]], [[Resolution|resolution]] 1.37&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1od1]] 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=1OD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OD1 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.37&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QS:N~2~-[(2R)-2-BENZYL-3-(TERT-BUTYLSULFONYL)PROPANOYL]-N-{(1R)-1-(CYCLOHEXYLMETHYL)-3,3-DIFLUORO-2,2-DIHYDROXY-4-[(2-MORPHOLIN-4-YLETHYL)AMINO]-4-OXOBUTYL}-3-(1H-IMIDAZOL-3-IUM-4-YL)-L-ALANINAMIDE'>0QS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1od1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1od1 OCA], [https://pdbe.org/1od1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1od1 RCSB], [https://www.ebi.ac.uk/pdbsum/1od1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1od1 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/od/1od1_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=1od1 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 has been anisotropically refined to a resolution of 1.37 A. The structure of this inhibitor complex is in agreement with previous structures of endothiapepsin gem-diol inhibitor complexes that have been used to develop proposed catalytic mechanisms. However, the increase in resolution over previous structures confirms the presence of a number of short hydrogen bonds within the active site that are likely to play an important role in the catalytic mechanism. The presence of low-barrier hydrogen bonds was indicated in a previous one-dimensional H NMR spectrum.


==About this Structure==
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A.,Coates L, Erskine PT, Mall S, Williams PA, Gill RS, Wood SP, Cooper JB Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):978-81. Epub 2003, May 23. PMID:12777758<ref>PMID:12777758</ref>
1OD1 is a [[http://en.wikipedia.org/wiki/Protein_complex Protein complex]] structure of sequences from [[http://en.wikipedia.org/wiki/Cryphonectria_parasitica Cryphonectria parasitica]] with SO4 as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OD1 OCA]].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The structure of endothiapepsin complexed with the gem-diol inhibitor PD-135,040 at 1.37 A., Coates L, Erskine PT, Mall S, Williams PA, Gill RS, Wood SP, Cooper JB, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):978-81. Epub 2003, May 23. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12777758 12777758]
</div>
<div class="pdbe-citations 1od1" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Pepsin|Pepsin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cryphonectria parasitica]]
[[Category: Cryphonectria parasitica]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Coates, L.]]
[[Category: Coates L]]
[[Category: Cooper, J.B.]]
[[Category: Cooper JB]]
[[Category: Erskine, P.T.]]
[[Category: Erskine PT]]
[[Category: Gill, R.S.]]
[[Category: Gill RS]]
[[Category: Mall, S.]]
[[Category: Mall S]]
[[Category: Wood, S.P.]]
[[Category: Wood SP]]
[[Category: SO4]]
[[Category: acid proteinase]]
[[Category: aspartyl protease]]
[[Category: hydrolase]]
[[Category: inhibitor]]
 
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Retrieved from "https://proteopedia.org/1od1"