1elc

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<StructureSection load='1elc' size='340' side='right'caption='[[1elc]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
<StructureSection load='1elc' size='340' side='right'caption='[[1elc]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1elc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pig Pig]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELC FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1elc]] 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=1ELC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELC 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=0Z3:6-AMMONIO-N-(TRIFLUOROACETYL)-L-NORLEUCYL-N-[4-(1-METHYLETHYL)PHENYL]-L-PHENYLALANINAMIDE'>0Z3</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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]] 1.75&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ela|1ela]], [[1elb|1elb]]</div></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=0Z3:6-AMMONIO-N-(TRIFLUOROACETYL)-L-NORLEUCYL-N-[4-(1-METHYLETHYL)PHENYL]-L-PHENYLALANINAMIDE'>0Z3</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1elc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elc OCA], [https://pdbe.org/1elc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elc RCSB], [https://www.ebi.ac.uk/pdbsum/1elc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elc 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=1elc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elc OCA], [https://pdbe.org/1elc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elc RCSB], [https://www.ebi.ac.uk/pdbsum/1elc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elc 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=1elc 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=1elc 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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It has been assumed that the structure of a single inhibitor complex is sufficient to define the available subsites of an enzyme that has a unique binding site and a uniquely defined mode for ligand binding--the specificity for these subsites can thus be probed by kinetic experiments. Elastase is an enzyme for which these traditional assumptions, which underlie such structural and kinetic studies, do not hold. Three new crystal structures of elastase complexed to chemically similar inhibitors with similar binding affinities reveal a diversity of binding modes as well as two new subsites on elastase. The existence of multiple binding sites and different binding modes for such similar inhibitors indicates that researchers must proceed with caution when using kinetics to map out protein subsites.
 
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Analogous inhibitors of elastase do not always bind analogously.,Mattos C, Rasmussen B, Ding X, Petsko GA, Ringe D Nat Struct Biol. 1994 Jan;1(1):55-8. PMID:7656008<ref>PMID:7656008</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 1elc" 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: Pig]]
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[[Category: Ding X]]
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[[Category: Ding, X]]
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[[Category: Mattos C]]
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[[Category: Mattos, C]]
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[[Category: Petsko GA]]
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[[Category: Petsko, G A]]
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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: Hydrolase-hydrolase inhibitor complex]]
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[[Category: Serine proteinase]]
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Revision as of 10:03, 20 March 2024

Analogous inhibitors of elastase do not always bind analogously

PDB ID 1elc

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