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[[Image:1c1m.jpg|left|200px]]
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{{STRUCTURE_1c1m|  PDB=1c1m  |  SCENE=  }}
'''PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)'''


==PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)==
<StructureSection load='1c1m' size='340' side='right'caption='[[1c1m]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== 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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG] Acts upon elastin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c1/1c1m_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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="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.


==Overview==
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>
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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1C1M 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=1C1M OCA].
</div>
<div class="pdbe-citations 1c1m" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/9443341 9443341]
*[[Elastase 3D structures|Elastase 3D structures]]
[[Category: Pancreatic elastase]]
== References ==
[[Category: Single protein]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Bourguet, W.]]
[[Category: Bourguet W]]
[[Category: Fourme, R.]]
[[Category: Colloc'h N]]
[[Category: H, N Colloc.]]
[[Category: Fourme R]]
[[Category: Longhi, S.]]
[[Category: Longhi S]]
[[Category: Pernot, L.]]
[[Category: Pernot L]]
[[Category: Prange, T.]]
[[Category: Prange T]]
[[Category: Schiltz, M.]]
[[Category: Schiltz M]]
[[Category: Hydrolase]]
[[Category: Pancreas elastase]]
[[Category: Serine protease]]
[[Category: Xenon]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:13:34 2008''

Latest revision as of 06:27, 30 October 2024

PORCINE ELASTASE UNDER XENON PRESSURE (8 BAR)

1c1m, resolution 2.20Å

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