1nes: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1nes]] is a 3 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=1NES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NES FirstGlance]. <br>
<table><tr><td colspan='2'>[[1nes]] is a 3 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=1NES OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NES FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<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>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nes OCA], [https://pdbe.org/1nes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nes RCSB], [https://www.ebi.ac.uk/pdbsum/1nes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nes 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=1nes FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nes OCA], [https://pdbe.org/1nes PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nes RCSB], [https://www.ebi.ac.uk/pdbsum/1nes PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nes ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG]] Acts upon elastin.  
[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=1nes 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=1nes ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A single crystal of porcine pancreatic elastase was mounted in a thin-walled capillary and allowed to react with acetyl-Ala-Pro-Ala-paranitroanalide. Diffraction data to 1.65 A resolution were measured and the isomorphous structure was solved from the difference Fourier map. The structure contains two surprises. Two molecules of the product: acetyl-Ala-Pro-Ala molecule are bound in the extended binding site. Both molecules are bound backwards with respect to the established mode of peptide binding.
Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 A resolution.,Meyer EF Jr, Radhakrishnan R, Cole GM, Presta LG J Mol Biol. 1986 Jun 5;189(3):533-9. PMID:3640831<ref>PMID:3640831</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1nes" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Elastase 3D structures|Elastase 3D structures]]
*[[Elastase 3D structures|Elastase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pancreatic elastase]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Cole, G M]]
[[Category: M Cole G]]
[[Category: Junior, E F.Meyer]]
[[Category: Meyer Junior EF]]
[[Category: Presta, L G]]
[[Category: Presta LG]]
[[Category: Radhakrishnan, R]]
[[Category: Radhakrishnan R]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Serine protease/inhibitor]]

Revision as of 11:48, 10 April 2024

STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTIONSTRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION

Structural highlights

1nes is a 3 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.65Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CELA1_PIG Acts upon elastin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1nes, resolution 1.65Å

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