1ufd: Difference between revisions
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<StructureSection load='1ufd' size='340' side='right'caption='[[1ufd]]' scene=''> | <StructureSection load='1ufd' size='340' side='right'caption='[[1ufd]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UFD FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1ufd FirstGlance], [https://www.ebi.ac.uk/pdbsum/1ufd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ufd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Latest revision as of 09:09, 6 October 2021
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COMPARATIVE MODELING OF NODULIN 26 FROM GLYCINE MAX.COMPARATIVE MODELING OF NODULIN 26 FROM GLYCINE MAX.
Structural highlights
Publication Abstract from PubMedA model of the nodulin 26 channel protein has been constructed based on comparative modeling and molecular dynamics simulations. Structural features of the protein indicate a selectivity filter that differs from those of the known structures of Escherichia coli glycerol facilitator and mammalian aquaporin 1. The model structure also reveals important roles of Ser207 and Phe96 in ligand binding and transport. Functional properties of soybean nodulin 26 from a comparative three-dimensional model.,Biswas S FEBS Lett. 2004 Jan 30;558(1-3):39-44. PMID:14759513[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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