1c1m
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1c1m]] 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=1C1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C1M FirstGlance]. <br> | <table><tr><td colspan='2'>[[1c1m]] 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=1C1M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1C1M 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>, <scene name='pdbligand=XE:XENON'>XE</scene | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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>, <scene name='pdbligand=XE:XENON'>XE</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=1c1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1m OCA], [https://pdbe.org/1c1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c1m RCSB], [https://www.ebi.ac.uk/pdbsum/1c1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1m 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=1c1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1c1m OCA], [https://pdbe.org/1c1m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1c1m RCSB], [https://www.ebi.ac.uk/pdbsum/1c1m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1c1m ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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=1c1m 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=1c1m ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | X-ray diffraction is used to study the binding of xenon and krypton to a variety of crystallised proteins: porcine pancreatic elastase; subtilisin Carlsberg from Bacillus licheniformis; cutinase from Fusarium solani; collagenase from Hypoderma lineatum; hen egg lysozyme, the lipoamide dehydrogenase domain from the outer membrane protein P64k from Neisseria meningitidis; urate-oxidase from Aspergillus flavus, mosquitocidal delta-endotoxin CytB from Bacillus thuringiensis and the ligand-binding domain of the human nuclear retinoid-X receptor RXR-alpha. Under gas pressures ranging from 8 to 20 bar, xenon is able to bind to discrete sites in hydrophobic cavities, ligand and substrate binding pockets, and into the pore of channel-like structures. These xenon complexes can be used to map hydrophobic sites in proteins, or as heavy-atom derivatives in the isomorphous replacement method of structure determination. | ||
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| - | Exploring hydrophobic sites in proteins with xenon or krypton.,Prange T, Schiltz M, Pernot L, Colloc'h N, Longhi S, Bourguet W, Fourme R Proteins. 1998 Jan;30(1):61-73. PMID:9443341<ref>PMID:9443341</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1c1m" 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: Bourguet | + | [[Category: Bourguet W]] |
| - | [[Category: Fourme | + | [[Category: Colloc'h N]] |
| - | [[Category: Longhi | + | [[Category: Fourme R]] |
| - | [[Category: Pernot | + | [[Category: Longhi S]] |
| - | [[Category: Prange | + | [[Category: Pernot L]] |
| - | [[Category: Schiltz | + | [[Category: Prange T]] |
| - | + | [[Category: Schiltz M]] | |
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Revision as of 15:37, 13 March 2024
PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)
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Categories: Large Structures | Sus scrofa | Bourguet W | Colloc'h N | Fourme R | Longhi S | Pernot L | Prange T | Schiltz M
