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[[Image:4er1.jpg|left|200px]]


{{Structure
==THE ACTIVE SITE OF ASPARTIC PROTEINASES==
|PDB= 4er1 |SIZE=350|CAPTION= <scene name='initialview01'>4er1</scene>, resolution 2.0&Aring;
<StructureSection load='4er1' size='340' side='right'caption='[[4er1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=BNA:BIS-(NAPHTHYL-1-METHYL)+ACETIC+ACID'>BNA</scene>, <scene name='pdbligand=CAL:5-AMINO-6-CYCLOHEXYL-4-HYDROXY-2-ISOBUTYL-HEXANOIC+ACID'>CAL</scene>, <scene name='pdbligand=DCI:2-METHYL-BUTYLAMINE'>DCI</scene>
<table><tr><td colspan='2'>[[4er1]] 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=4ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ER1 FirstGlance]. <br>
|ACTIVITY= <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, 3.4.23.28 and 3.4.23.30 3.4.21.103, 3.4.23.18, 3.4.23.28 and 3.4.23.30] </span>
</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>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4er1 OCA], [https://pdbe.org/4er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4er1 RCSB], [https://www.ebi.ac.uk/pdbsum/4er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4er1 ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/4er1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=4er1 RCSB]</span>
== Evolutionary Conservation ==
}}
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
'''THE ACTIVE SITE OF ASPARTIC PROTEINASES'''
  <jmolCheckbox>
 
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/er/4er1_consurf.spt"</scriptWhenChecked>
 
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
==Overview==
    <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=4er1 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 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.


==About this Structure==
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>
4ER1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ER1 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
The active site of aspartic proteinases., Pearl L, Blundell T, FEBS Lett. 1984 Aug 20;174(1):96-101. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/6381096 6381096]
</div>
[[Category: Hydrolase]]
<div class="pdbe-citations 4er1" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
[[Category: Blundell, T L.]]
[[Category: Cooper, J B.]]
[[Category: Quail, J W.]]
[[Category: Szelke, M.]]
[[Category: hydrolase (acid proteinase)]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:38:36 2008''
==See Also==
*[[Pepsin|Pepsin]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cryphonectria parasitica]]
[[Category: Large Structures]]
[[Category: Blundell TL]]
[[Category: Cooper JB]]
[[Category: Quail JW]]
[[Category: Szelke M]]
Retrieved from "https://proteopedia.org/4er1"