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[[Image:2nnl.jpg|left|200px]]


{{Structure
==Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site==
|PDB= 2nnl |SIZE=350|CAPTION= <scene name='initialview01'>2nnl</scene>, resolution 2.100&Aring;
<StructureSection load='2nnl' size='340' side='right'caption='[[2nnl]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|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>
<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>
|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>
</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>
|GENE= dfr1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29760 Vitis vinifera])
<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>
|DOMAIN=
<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>
|RELATEDENTRY=[[2c29|2c29]]
</table>
|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>
== Function ==
}}
[https://www.uniprot.org/uniprot/DFRA_VITVI DFRA_VITVI] Bifunctional enzyme involved in flavonoid metabolism.[UniProtKB:Q9XES5]
 
== Evolutionary Conservation ==
'''Binding of two substrate analogue molecules to dihydroflavonol-4-reductase alters the functional geometry of the catalytic site'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==About this Structure==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nn/2nnl_consurf.spt"</scriptWhenChecked>
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].  
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
[[Category: Dihydrokaempferol 4-reductase]]
    <text>to colour the structure by Evolutionary Conservation</text>
[[Category: Single protein]]
  </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=2nnl ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Vitis vinifera]]
[[Category: Vitis vinifera]]
[[Category: Estaintot, B Langlois D.]]
[[Category: Gallois B]]
[[Category: Gallois, B.]]
[[Category: Granier T]]
[[Category: Granier, T.]]
[[Category: Langlois D'Estaintot B]]
[[Category: Petit, P.]]
[[Category: Petit P]]
[[Category: oxidoreductase]]
[[Category: rossmann fold]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:05:37 2008''

Latest revision as of 08:54, 25 October 2023

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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