1uo6: Difference between revisions
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< | ==PORCINE PANCREATIC ELASTASE/Xe-COMPLEX== | ||
<StructureSection load='1uo6' size='340' side='right'caption='[[1uo6]], [[Resolution|resolution]] 1.65Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1uo6]] 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=1UO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UO6 FirstGlance]. <br> | |||
or | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=1uo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uo6 OCA], [https://pdbe.org/1uo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uo6 RCSB], [https://www.ebi.ac.uk/pdbsum/1uo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uo6 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/uo/1uo6_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1uo6 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Complete and highly redundant data sets were collected at nine different wavelengths between 0.80 and 2.65 A on a xenon derivative of porcine pancreatic elastase in both air and helium atmospheres. The magnitude of the anomalous signal, as assessed by the xenon-peak height in the anomalous difference Patterson synthesis, is affected by the wavelength of data collection as well as by the scaling model used. For data collected at wavelengths longer than 1.7 A, the use of a three-dimensional scaling protocol is essential in order to obtain the highest possible anomalous signal. Based on the scaling protocols currently available, the optimal wavelength range for data collection appears to be between 2.1 and 2.4 A. Beyond that, any further increase in signal will be compensated for or even superseded by a concomitant increase in noise, which cannot be fully corrected for. Data collection in a helium atmosphere yields higher I/sigma(I) values, but not significantly better anomalous differences, than data collection in air. | |||
On the routine use of soft X-rays in macromolecular crystallography. Part II. Data-collection wavelength and scaling models.,Mueller-Dieckmann C, Polentarutti M, Djinovic Carugo K, Panjikar S, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):28-38. Epub 2003, Dec 18. PMID:14684889<ref>PMID:14684889</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uo6" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Elastase 3D structures|Elastase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
< | |||
[[Category: | |||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
[[Category: Djinovic-Carugo | [[Category: Djinovic-Carugo K]] | ||
[[Category: Mueller-Dieckmann | [[Category: Mueller-Dieckmann C]] | ||
[[Category: Panjikar | [[Category: Panjikar S]] | ||
[[Category: Polentarutti | [[Category: Polentarutti M]] | ||
[[Category: Tucker | [[Category: Tucker PA]] | ||
[[Category: Weiss | [[Category: Weiss MS]] | ||
Latest revision as of 15:53, 13 December 2023
PORCINE PANCREATIC ELASTASE/Xe-COMPLEXPORCINE PANCREATIC ELASTASE/Xe-COMPLEX
Structural highlights
FunctionCELA1_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. Publication Abstract from PubMedComplete and highly redundant data sets were collected at nine different wavelengths between 0.80 and 2.65 A on a xenon derivative of porcine pancreatic elastase in both air and helium atmospheres. The magnitude of the anomalous signal, as assessed by the xenon-peak height in the anomalous difference Patterson synthesis, is affected by the wavelength of data collection as well as by the scaling model used. For data collected at wavelengths longer than 1.7 A, the use of a three-dimensional scaling protocol is essential in order to obtain the highest possible anomalous signal. Based on the scaling protocols currently available, the optimal wavelength range for data collection appears to be between 2.1 and 2.4 A. Beyond that, any further increase in signal will be compensated for or even superseded by a concomitant increase in noise, which cannot be fully corrected for. Data collection in a helium atmosphere yields higher I/sigma(I) values, but not significantly better anomalous differences, than data collection in air. On the routine use of soft X-rays in macromolecular crystallography. Part II. Data-collection wavelength and scaling models.,Mueller-Dieckmann C, Polentarutti M, Djinovic Carugo K, Panjikar S, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):28-38. Epub 2003, Dec 18. PMID:14684889[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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