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==Crystal structure of a mammalian reductase==
==Crystal structure of a mammalian reductase==
<StructureSection load='2zat' size='340' side='right' caption='[[2zat]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='2zat' size='340' side='right'caption='[[2zat]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2zat]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ZAT FirstGlance]. <br>
<table><tr><td colspan='2'>[[2zat]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ZAT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ZAT 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></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbonyl_reductase_(NADPH) Carbonyl reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.184 1.1.1.184] </span></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></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=2zat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zat OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2zat RCSB], [http://www.ebi.ac.uk/pdbsum/2zat PDBsum]</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=2zat FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2zat OCA], [https://pdbe.org/2zat PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2zat RCSB], [https://www.ebi.ac.uk/pdbsum/2zat PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2zat ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DHRS4_PIG DHRS4_PIG]] Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.<ref>PMID:12604222</ref>
[https://www.uniprot.org/uniprot/DHRS4_PIG DHRS4_PIG] Reduces all-trans-retinal and 9-cis retinal. Can also catalyze the oxidation of all-trans-retinol with NADP as co-factor, but with much lower efficiency. Reduces alkyl phenyl ketones and alpha-dicarbonyl compounds with aromatic rings, such as pyrimidine-4-aldehyde, 3-benzoylpyridine, 4-benzoylpyridine, menadione and 4-hexanoylpyridine. Has no activity towards aliphatic aldehydes and ketones.<ref>PMID:12604222</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zat_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/za/2zat_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=2zat ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 2zat" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Aoki, K]]
[[Category: Aoki K]]
[[Category: Nakamura, K T]]
[[Category: Nakamura KT]]
[[Category: Tanaka, N]]
[[Category: Tanaka N]]
[[Category: Alpha/beta]]
[[Category: Oxidoreductase]]
Retrieved from "https://proteopedia.org/2zat"