4dyd

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dyd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi Acinetobacter baylyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DYD FirstGlance]. <br>
<table><tr><td colspan='2'>[[4dyd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baylyi Acinetobacter baylyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DYD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4DYD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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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]] 1.95&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyd OCA], [https://pdbe.org/4dyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dyd RCSB], [https://www.ebi.ac.uk/pdbsum/4dyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyd ProSAT]</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=4dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyd OCA], [https://pdbe.org/4dyd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4dyd RCSB], [https://www.ebi.ac.uk/pdbsum/4dyd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyd ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/B1P3E1_ACIBI B1P3E1_ACIBI]]
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[https://www.uniprot.org/uniprot/B1P3E1_ACIBI B1P3E1_ACIBI]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Diketoreductase catalyzes a two-step bioreduction on a dicarbonyl substrate through a novel dual catalysis mode, in which random hydride attack simultaneously forms two mono-carbonyl intermediates, and subsequently distinct catalytic sites are responsible for the reductions of respective carbonyl group of the intermediates to yield the final dihydroxy product.
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Dual catalysis mode for the dicarbonyl reduction catalyzed by diketoreductase.,Lu M, Huang Y, White MA, Wu X, Liu N, Cheng X, Chen Y Chem Commun (Camb). 2012 Oct 24;48(92):11352-4. doi: 10.1039/c2cc36334h. PMID:23073461<ref>PMID:23073461</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4dyd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductase

PDB ID 4dyd

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