1elf

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<StructureSection load='1elf' size='340' side='right'caption='[[1elf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1elf' size='340' side='right'caption='[[1elf]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1elf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1elf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELF FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BAF:(TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO+ETHYL-FORMAMIDE'>BAF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></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=BAF:(TERT-BUTYLOXYCARBONYL)-ALANYL-AMINO+ETHYL-FORMAMIDE'>BAF</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1elf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elf OCA], [https://pdbe.org/1elf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elf RCSB], [https://www.ebi.ac.uk/pdbsum/1elf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elf ProSAT]</span></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=1elf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elf OCA], [https://pdbe.org/1elf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elf RCSB], [https://www.ebi.ac.uk/pdbsum/1elf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG]] Acts upon elastin.
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[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1elf ConSurf].
</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=1elf ConSurf].
<div style="clear:both"></div>
<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 mechanism of inactivation of porcine pancreatic elastase (PPE) by N-peptidyl-O-aroylhydroxylamine was studied by X-ray crystallography. The inactivator forms a stable complex with the enzyme by means of a covalent attachment to the active site Ser 203(195) O gamma. The nature of the complex is, however, different depending on the pH at which the inactivation reaction occurs. At pH 5, the complex formed is a hydroxylamine derivative of Ser 203(195) in which the O gamma of serine is the oxygen of the hydroxylamine derivative. At pH 7.5, the complex formed is a carbamate derivative at Ser 203(195) O gamma. In both types of complexes, the inactivator binds in the S' subsites of the enzyme instead of forming the usual antiparallel beta-sheet with the S subsites. The implication for the mechanism of inactivation at different pHs is discussed.
 
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Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pH.,Ding X, Rasmussen BF, Demuth HU, Ringe D, Steinmetz AC Biochemistry. 1995 Jun 13;34(23):7749-56. PMID:7779821<ref>PMID:7779821</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 1elf" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
*[[Elastase 3D structures|Elastase 3D structures]]
*[[Elastase 3D structures|Elastase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Pancreatic elastase]]
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[[Category: Sus scrofa]]
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[[Category: Demuth, H U]]
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[[Category: Demuth H-U]]
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[[Category: Ding, X]]
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[[Category: Ding X]]
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[[Category: Rasmussen, B]]
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[[Category: Rasmussen B]]
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[[Category: Ringe, D]]
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[[Category: Ringe D]]
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[[Category: Steinmetz, A C.U]]
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[[Category: Steinmetz ACU]]

Revision as of 10:03, 20 March 2024

NATURE OF THE INACTIVATION OF ELASTASE BY N-PEPTIDYL-O-AROYL HYDROXYLAMINE AS A FUNCTION OF PH

PDB ID 1elf

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