3caq

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{{STRUCTURE_3caq| PDB=3caq | SCENE= }}
 
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===Crystal structure of 5beta-reductase (AKR1D1) in complex with NADPH===
 
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{{ABSTRACT_PUBMED_19075558}}
 
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==Disease==
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==Crystal structure of 5beta-reductase (AKR1D1) in complex with NADPH==
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[[http://www.uniprot.org/uniprot/AK1D1_HUMAN AK1D1_HUMAN]] Defects in AKR1D1 are the cause of congenital bile acid synthesis defect type 2 (CBAS2) [MIM:[http://omim.org/entry/235555 235555]]; also known as cholestasis with delta(4)-3-oxosteroid 5-beta-reductase deficiency. Patients with this liver disease show absence or low levels of chenodeoxycholic acid and cholic acid in plasma and urine.<ref>PMID:12970144</ref><ref>PMID:15030995</ref>
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<StructureSection load='3caq' size='340' side='right'caption='[[3caq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3caq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CAQ FirstGlance]. <br>
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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]] 2.2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=NDP:NADPH+DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NDP</scene></td></tr>
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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=3caq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3caq OCA], [https://pdbe.org/3caq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3caq RCSB], [https://www.ebi.ac.uk/pdbsum/3caq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3caq ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/AK1D1_HUMAN AK1D1_HUMAN] Defects in AKR1D1 are the cause of congenital bile acid synthesis defect type 2 (CBAS2) [MIM:[https://omim.org/entry/235555 235555]; also known as cholestasis with delta(4)-3-oxosteroid 5-beta-reductase deficiency. Patients with this liver disease show absence or low levels of chenodeoxycholic acid and cholic acid in plasma and urine.<ref>PMID:12970144</ref> <ref>PMID:15030995</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/AK1D1_HUMAN AK1D1_HUMAN] Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.
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== Evolutionary Conservation ==
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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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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ca/3caq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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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=3caq ConSurf].
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<div style="clear:both"></div>
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==Function==
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==See Also==
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[[http://www.uniprot.org/uniprot/AK1D1_HUMAN AK1D1_HUMAN]] Efficiently catalyzes the reduction of progesterone, androstenedione, 17-alpha-hydroxyprogesterone and testosterone to 5-beta-reduced metabolites. The bile acid intermediates 7-alpha,12-alpha-dihydroxy-4-cholesten-3-one and 7-alpha-hydroxy-4-cholesten-3-one can also act as substrates.
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*[[Aldo-keto reductase 3D structures|Aldo-keto reductase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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[[3caq]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CAQ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:019075558</ref><references group="xtra"/><references/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Breton, R]]
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[[Category: Large Structures]]
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[[Category: Cantin, L]]
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[[Category: Breton R]]
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[[Category: Faucher, F]]
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[[Category: Cantin L]]
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[[Category: 5b-dhp]]
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[[Category: Faucher F]]
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[[Category: 5b-red]]
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[[Category: 5b-reductase]]
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[[Category: 5beta-reductase]]
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[[Category: Akr]]
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[[Category: Akr1d1]]
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[[Category: Aldo-keto reductase]]
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[[Category: Androstenedione]]
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[[Category: Bile acid catabolism]]
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[[Category: Disease mutation]]
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[[Category: Lipid metabolism]]
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[[Category: Nadp]]
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[[Category: Nadph]]
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[[Category: Oxidoreductase]]
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[[Category: Steroid metabolism]]
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[[Category: Substrate inhibition]]
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Current revision

Crystal structure of 5beta-reductase (AKR1D1) in complex with NADPH

PDB ID 3caq

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