2iod
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2iod]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IOD FirstGlance]. <br> | <table><tr><td colspan='2'>[[2iod]] is a 4 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2IOD FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dfr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Vitis vinifera])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dfr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Vitis vinifera])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrokaempferol_4-reductase Dihydrokaempferol 4-reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.219 1.1.1.219] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dihydrokaempferol_4-reductase Dihydrokaempferol 4-reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.219 1.1.1.219] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iod RCSB], [http://www.ebi.ac.uk/pdbsum/2iod PDBsum]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2iod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iod OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2iod RCSB], [http://www.ebi.ac.uk/pdbsum/2iod PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Dihydrokaempferol 4-reductase]] | [[Category: Dihydrokaempferol 4-reductase]] | ||
[[Category: Vitis vinifera]] | [[Category: Vitis vinifera]] | ||
| - | [[Category: Estaintot, B Langlois d | + | [[Category: Estaintot, B Langlois d]] |
| - | [[Category: Gallois, B | + | [[Category: Gallois, B]] |
| - | [[Category: Granier, T | + | [[Category: Granier, T]] |
| - | [[Category: Petit, P | + | [[Category: Petit, P]] |
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Rossmann fold]] | [[Category: Rossmann fold]] | ||
Revision as of 08:20, 16 January 2015
Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site
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