1uvo
From Proteopedia
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| - | [[ | + | ==STRUCTURE OF THE COMPLEX OF PORCINE PANCREATIC ELASTASE IN COMPLEX WITH CADMIUM REFINED AT 1.85 A RESOLUTION (CRYSTAL A)== |
| + | <StructureSection load='1uvo' size='340' side='right' caption='[[1uvo]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1uvo]] is a 1 chain structure with 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=1UVO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UVO FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1b0e|1b0e]], [[1bma|1bma]], [[1btu|1btu]], [[1c1m|1c1m]], [[1e34|1e34]], [[1e35|1e35]], [[1e36|1e36]], [[1e37|1e37]], [[1e38|1e38]], [[1eai|1eai]], [[1eas|1eas]], [[1eat|1eat]], [[1eau|1eau]], [[1ela|1ela]], [[1elb|1elb]], [[1elc|1elc]], [[1eld|1eld]], [[1ele|1ele]], [[1elf|1elf]], [[1elg|1elg]], [[1esa|1esa]], [[1esb|1esb]], [[1est|1est]], [[1fle|1fle]], [[1fzz|1fzz]], [[1gvk|1gvk]], [[1gwa|1gwa]], [[1h9l|1h9l]], [[1hax|1hax]], [[1hay|1hay]], [[1haz|1haz]], [[1hb0|1hb0]], [[1hv7|1hv7]], [[1inc|1inc]], [[1jim|1jim]], [[1l0z|1l0z]], [[1l1g|1l1g]], [[1lka|1lka]], [[1lkb|1lkb]], [[1lvy|1lvy]], [[1mcv|1mcv]], [[1mmj|1mmj]], [[1nes|1nes]], [[1okx|1okx]], [[1qgf|1qgf]], [[1qix|1qix]], [[1qnj|1qnj]], [[1qr3|1qr3]], [[1uo6|1uo6]], [[2est|2est]], [[3est|3est]], [[4est|4est]], [[5est|5est]], [[6est|6est]], [[7est|7est]], [[8est|8est]], [[9est|9est]], [[1uvp|1uvp]]</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1uvo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uvo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1uvo RCSB], [http://www.ebi.ac.uk/pdbsum/1uvo PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == 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/uv/1uvo_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Two series of complete and highly redundant data sets were collected at wavelengths of 1.00 and 2.00 Angstroms on a cadmium derivative of porcine pancreatic elastase (PPE). Radiation damage to the sample was evaluated qualitatively by inspecting consecutive difference electron density maps during the course of the experiment. The nature of the radiation damage was found to be identical at both wavelengths and was localized primarily at the four disulfide bridges of PPE, the cadmium site and the two methionine residues. For a quantitative examination of the radiation damage, the decrease in the peak height of the cadmium ion in various electron density maps was exploited. Again, no significant difference in radiation damage between the two wavelengths was observed. This can be rationalized by considering the wavelength dependencies of the number of diffracted photons versus the number of absorbed photons and the energy deposited in the crystal by the latter. | ||
| - | + | On the influence of the incident photon energy on the radiation damage in crystalline biological samples.,Weiss MS, Panjikar S, Mueller-Dieckmann C, Tucker PA J Synchrotron Radiat. 2005 May;12(Pt 3):304-9. Epub 2005 Apr 14. PMID:15840915<ref>PMID:15840915</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Elastase|Elastase]] | *[[Elastase|Elastase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Pancreatic elastase]] | [[Category: Pancreatic elastase]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
Revision as of 19:36, 28 September 2014
STRUCTURE OF THE COMPLEX OF PORCINE PANCREATIC ELASTASE IN COMPLEX WITH CADMIUM REFINED AT 1.85 A RESOLUTION (CRYSTAL A)
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