2nnl

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[[Image:2nnl.jpg|left|200px]]
 
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{{Structure
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==Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site==
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|PDB= 2nnl |SIZE=350|CAPTION= <scene name='initialview01'>2nnl</scene>, resolution 2.100&Aring;
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<StructureSection load='2nnl' size='340' side='right'caption='[[2nnl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>
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<table><tr><td colspan='2'>[[2nnl]] is a 2 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=2NNL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NNL FirstGlance]. <br>
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|ACTIVITY= <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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
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|GENE= dfr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Vitis vinifera])
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=[[2c29|2c29]]
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</table>
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|RESOURCES=<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://www.ebi.ac.uk/pdbsum/2nnl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2nnl RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/DFRA_VITVI DFRA_VITVI] Bifunctional enzyme involved in flavonoid metabolism.[UniProtKB:Q9XES5]
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== Evolutionary Conservation ==
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'''Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/2nnl_consurf.spt"</scriptWhenChecked>
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2NNL is a [[Single protein]] structure of 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=2NNL OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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[[Category: Dihydrokaempferol 4-reductase]]
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<text>to colour the structure by Evolutionary Conservation</text>
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[[Category: Single protein]]
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</jmolCheckbox>
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</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=2nnl ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Vitis vinifera]]
[[Category: Vitis vinifera]]
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[[Category: Estaintot, B Langlois D.]]
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[[Category: Gallois B]]
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[[Category: Gallois, B.]]
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[[Category: Granier T]]
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[[Category: Granier, T.]]
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[[Category: Langlois D'Estaintot B]]
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[[Category: Petit, P.]]
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[[Category: Petit P]]
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[[Category: oxidoreductase]]
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[[Category: rossmann fold]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:05:37 2008''
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Current revision

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

PDB ID 2nnl

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