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3bxx
From Proteopedia
(Difference between revisions)
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==Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of the catalytic site== | ==Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of the catalytic site== | ||
| - | <StructureSection load='3bxx' size='340' side='right' caption='[[3bxx]], [[Resolution|resolution]] 2.90Å' scene=''> | + | <StructureSection load='3bxx' size='340' side='right'caption='[[3bxx]], [[Resolution|resolution]] 2.90Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3bxx]] is a 6 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3bxx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Grape Grape]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BXX FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=QUE:3,5,7,3,4-PENTAHYDROXYFLAVONE'>QUE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=QUE:3,5,7,3,4-PENTAHYDROXYFLAVONE'>QUE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2iod|2iod]], [[3c1t|3c1t]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2iod|2iod]], [[3c1t|3c1t]]</div></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DFR1 ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DFR1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Grape])</td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Dihydrokaempferol_4-reductase Dihydrokaempferol 4-reductase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.219 1.1.1.219] </span></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=3bxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bxx OCA], [https://pdbe.org/3bxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bxx RCSB], [https://www.ebi.ac.uk/pdbsum/3bxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bxx ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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==See Also== | ==See Also== | ||
| - | *[[Ion channels|Ion channels]] | + | *[[Ion channels 3D structures|Ion channels 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
| Line 38: | Line 38: | ||
[[Category: Dihydrokaempferol 4-reductase]] | [[Category: Dihydrokaempferol 4-reductase]] | ||
[[Category: Grape]] | [[Category: Grape]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Delrot, S]] | [[Category: Delrot, S]] | ||
[[Category: Estaintot, B Langlois d]] | [[Category: Estaintot, B Langlois d]] | ||
Revision as of 08:28, 19 January 2022
Binding of two substrate analogue molecules to dihydroflavonol 4-reductase alters the functional geometry of the catalytic site
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