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.
2iod
From Proteopedia
(Difference between revisions)
| (12 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2iod.jpg|left|200px]]<br /><applet load="2iod" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2iod, resolution 2.060Å" /> | ||
| - | '''Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site'''<br /> | ||
| - | == | + | ==Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site== |
| - | + | <StructureSection load='2iod' size='340' side='right'caption='[[2iod]], [[Resolution|resolution]] 2.06Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | [[Category: | + | <table><tr><td colspan='2'>[[2iod]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Vitis_vinifera Vitis vinifera]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IOD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IOD 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]] 2.06Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MYC:3,5,7-TRIHYDROXY-2-(3,4,5-TRIHYDROXYPHENYL)-4H-CHROMEN-4-ONE'>MYC</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=2iod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iod OCA], [https://pdbe.org/2iod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iod RCSB], [https://www.ebi.ac.uk/pdbsum/2iod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iod ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DFRA_VITVI DFRA_VITVI] Bifunctional enzyme involved in flavonoid metabolism.[UniProtKB:Q9XES5] | ||
| + | == 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/io/2iod_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=2iod ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Vitis vinifera]] | [[Category: Vitis vinifera]] | ||
| - | + | [[Category: Gallois B]] | |
| - | [[Category: Gallois | + | [[Category: Granier T]] |
| - | [[Category: Granier | + | [[Category: Langlois d'Estaintot B]] |
| - | [[Category: | + | [[Category: Petit P]] |
| - | [[Category: | + | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
Current revision
Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site
| |||||||||||

