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==Studies on DCR shed new light on peroxisomal beta-oxidation: Crystal structure of the ternary complex of pDCR==
==Studies on DCR shed new light on peroxisomal beta-oxidation: Crystal structure of the ternary complex of pDCR==
<StructureSection load='4fc7' size='340' side='right' caption='[[4fc7]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
<StructureSection load='4fc7' size='340' side='right'caption='[[4fc7]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4fc7]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FC7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4FC7 FirstGlance]. <br>
<table><tr><td colspan='2'>[[4fc7]] is a 4 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=4FC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FC7 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</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=COA:COENZYME+A'>COA</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">[[4fc6|4fc6]]</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=4fc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fc7 OCA], [https://pdbe.org/4fc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fc7 RCSB], [https://www.ebi.ac.uk/pdbsum/4fc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fc7 ProSAT]</span></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DECR2, PDCR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/2,4-dienoyl-CoA_reductase_(NADPH) 2,4-dienoyl-CoA reductase (NADPH)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.1.34 1.3.1.34] </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=4fc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fc7 OCA], [http://pdbe.org/4fc7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4fc7 RCSB], [http://www.ebi.ac.uk/pdbsum/4fc7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4fc7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DECR2_HUMAN DECR2_HUMAN]] Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.  
[https://www.uniprot.org/uniprot/DECR2_HUMAN DECR2_HUMAN] Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Hua, T]]
[[Category: Large Structures]]
[[Category: Liu, Z J]]
[[Category: Hua T]]
[[Category: Shaw, N]]
[[Category: Liu Z-J]]
[[Category: Wang, J]]
[[Category: Shaw N]]
[[Category: Wu, D]]
[[Category: Wang J]]
[[Category: Oxidoreductase]]
[[Category: Wu D]]
[[Category: Peroxisomal beta-oxidation]]
[[Category: Sdr/rossmann fold]]
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