2nnl: Difference between revisions

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<StructureSection load='2nnl' size='340' side='right'caption='[[2nnl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='2nnl' size='340' side='right'caption='[[2nnl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2nnl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Grape Grape]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NNL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2NNL FirstGlance]. <br>
<table><tr><td colspan='2'>[[2nnl]] is a 2 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=2NNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ERD:(2S)-2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>ERD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ERD:(2S)-2-(3,4-DIHYDROXYPHENYL)-5,7-DIHYDROXY-2,3-DIHYDRO-4H-CHROMEN-4-ONE'>ERD</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2c29|2c29]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2c29|2c29]]</div></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 Grape])</td></tr>
<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'>[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'>[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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2nnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnl OCA], [http://pdbe.org/2nnl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2nnl RCSB], [http://www.ebi.ac.uk/pdbsum/2nnl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnl ProSAT]</span></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=2nnl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2nnl OCA], [https://pdbe.org/2nnl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2nnl RCSB], [https://www.ebi.ac.uk/pdbsum/2nnl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2nnl ProSAT]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==

Revision as of 20:50, 20 October 2021

Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site

2nnl, resolution 2.10Å

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