This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1dla
From Proteopedia
(Difference between revisions)
| (14 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:1dla.jpg|left|200px]] | ||
| - | + | ==NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE== | |
| - | + | <StructureSection load='1dla' size='340' side='right'caption='[[1dla]], [[Resolution|resolution]] 3.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1dla]] is a 4 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=1DLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DLA 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]] 3Å</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=1dla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dla OCA], [https://pdbe.org/1dla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dla RCSB], [https://www.ebi.ac.uk/pdbsum/1dla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dla ProSAT]</span></td></tr> |
| - | + | </table> | |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ALDR_PIG ALDR_PIG] Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols with a broad range of catalytic efficiencies. | ||
| + | == 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/dl/1dla_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=1dla ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | + | ==See Also== | |
| - | + | *[[Aldose reductase 3D structures|Aldose reductase 3D structures]] | |
| - | + | __TOC__ | |
| - | == | + | </StructureSection> |
| - | Aldose reductase | + | [[Category: Large Structures]] |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | [[Category: | + | |
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
| - | [[Category: Barth | + | [[Category: Barth P]] |
| - | [[Category: Biellmann | + | [[Category: Biellmann J-F]] |
| - | [[Category: Moras | + | [[Category: Moras D]] |
| - | [[Category: Podjarny | + | [[Category: Podjarny A]] |
| - | [[Category: Reymann | + | [[Category: Reymann J-M]] |
| - | [[Category: Rondeau | + | [[Category: Rondeau J-M]] |
| - | [[Category: Tete-Favier | + | [[Category: Tete-Favier F]] |
| - | + | ||
Current revision
NOVEL NADPH-BINDING DOMAIN REVEALED BY THE CRYSTAL STRUCTURE OF ALDOSE REDUCTASE
| |||||||||||

