1zir: Difference between revisions
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<StructureSection load='1zir' size='340' side='right'caption='[[1zir]], [[Resolution|resolution]] 1.36Å' scene=''> | <StructureSection load='1zir' size='340' side='right'caption='[[1zir]], [[Resolution|resolution]] 1.36Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1zir]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1zir]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZIR FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a5d|1a5d]], [[1zgt|1zgt]], [[1zie|1zie]], [[1ziq|1ziq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a5d|1a5d]], [[1zgt|1zgt]], [[1zie|1zie]], [[1ziq|1ziq]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zir OCA], [https://pdbe.org/1zir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zir RCSB], [https://www.ebi.ac.uk/pdbsum/1zir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zir ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/CRGE_RAT CRGE_RAT]] Crystallins are the dominant structural components of the vertebrate eye lens. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 11:21, 10 November 2021
Deuterated gammaE crystallin in H2O solventDeuterated gammaE crystallin in H2O solvent
Structural highlights
Function[CRGE_RAT] Crystallins are the dominant structural components of the vertebrate eye lens. 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 PubMedRat gammaE-crystallin was overexpressed, purified under different labelling conditions and crystallized and X-ray data were collected at resolutions between 1.71 and 1.36 A. The structures were determined by molecular replacement. In these structures, the cd loop of the Greek-key motif 3, which is the major structural key motif of the two phase-transition groups of gamma-crystallins, presents a double conformation. The influence of the perdeuteration on the protein structure was determined by comparison of the atomic positions and temperature factors of the different models. The perdeuterated proteins have a similar structure to their hydrogenated counterparts, but partial or full deuteration may have some effect on the atomic B-factor values. A comparison of refined X-ray structures of hydrogenated and perdeuterated rat gammaE-crystallin in H2O and D2O.,Artero JB, Hartlein M, McSweeney S, Timmins P Acta Crystallogr D Biol Crystallogr. 2005 Nov;61(Pt 11):1541-9. Epub 2005, Oct 19. PMID:16239733[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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