1elt
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1elt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmo_salar Salmo salar]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELT FirstGlance]. <br> | <table><tr><td colspan='2'>[[1elt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmo_salar Salmo salar]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ELT FirstGlance]. <br> | ||
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.61Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</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=1elt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elt OCA], [https://pdbe.org/1elt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elt RCSB], [https://www.ebi.ac.uk/pdbsum/1elt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elt 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=1elt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elt OCA], [https://pdbe.org/1elt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1elt RCSB], [https://www.ebi.ac.uk/pdbsum/1elt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1elt ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ELA1_SALSA ELA1_SALSA] Acts upon elastin.<ref>PMID:9628006</ref> | |
== 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=1elt 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=1elt ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The crystal structure of native salmon pancreatic elastase (SPE) has been solved by molecular-replacement methods, and refined by conventional conjugate-gradient methods and simulated-annealing techniques. The final R value is 17.2% for 21 389 reflections between 8.0 and 1.61 A, and the corresponding free R value is 23.9%. The overall tertiary structure of SPE is remarkably similar to that of porcine pancreatic elastase I (PPE), to which it shows about 67% sequence identity. The primary structure of SPE is determined from the electron-density maps, and only about 15 side chains are somewhat uncertain. Interesting differences between SPE and PPE, are one sequence deletion assigned to position 186, the residue 192 at the entrance of the specificity pocket is substituted from a Gln in PPE to Asn in SPE, and one of the calcium ligands is different. Furthermore, electron density is missing in SPE for the last three residues of the C-terminal helix. A comparison of the present amino-acid sequence of SPE with other sequences available indicates that SPE belongs to the class 1 pancreatic elastases. | ||
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| - | Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution.,Berglund GI, Willassen NP, Hordvik A, Smalas AO Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):925-37. PMID:15299762<ref>PMID:15299762</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1elt" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Pancreatic elastase]] | ||
[[Category: Salmo salar]] | [[Category: Salmo salar]] | ||
| - | [[Category: Berglund | + | [[Category: Berglund GI]] |
| - | [[Category: Smalaas | + | [[Category: Smalaas AO]] |
| - | + | ||
Revision as of 10:04, 20 March 2024
STRUCTURE OF NATIVE PANCREATIC ELASTASE FROM NORTH ATLANTIC SALMON AT 1.61 ANGSTROMS RESOLUTION
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