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1nes

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[[Image:1nes.jpg|left|200px]]
 
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{{Structure
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==STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION==
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|PDB= 1nes |SIZE=350|CAPTION= <scene name='initialview01'>1nes</scene>, resolution 1.65&Aring;
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<StructureSection load='1nes' size='340' side='right'caption='[[1nes]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
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<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>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36]
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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]] 1.65&#8491;</td></tr>
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|GENE=
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<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>
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}}
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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=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>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ne/1nes_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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].
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<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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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.
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'''STRUCTURE OF THE PRODUCT COMPLEX OF ACETYL-ALA-PRO-ALA WITH PORCINE PANCREATIC ELASTASE AT 1.65 ANGSTROMS RESOLUTION'''
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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>
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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 1nes" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Elastase 3D structures|Elastase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1NES is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/3640831 3640831]
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[[Category: Pancreatic elastase]]
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[[Category: Single protein]]
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
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[[Category: Cole, G M.]]
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[[Category: M Cole G]]
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[[Category: Junior, E F.Meyer.]]
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[[Category: Meyer Junior EF]]
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[[Category: Presta, L G.]]
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[[Category: Presta LG]]
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[[Category: Radhakrishnan, R.]]
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[[Category: Radhakrishnan R]]
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[[Category: ACE]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: complex (serine protease/inhibitor)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:55:55 2008''
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Current revision

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

PDB ID 1nes

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