4dyd: Difference between revisions

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<StructureSection load='4dyd' size='340' side='right'caption='[[4dyd]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='4dyd' size='340' side='right'caption='[[4dyd]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4dyd]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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>
</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>
<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=4dyd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dyd OCA], [http://pdbe.org/4dyd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4dyd RCSB], [http://www.ebi.ac.uk/pdbsum/4dyd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4dyd ProSAT]</span></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>
<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>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/B1P3E1_ACIBI B1P3E1_ACIBI]
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.
 
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>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4dyd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acinetobacter baylyi]]
[[Category: Acinetobacter baylyi]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, Y]]
[[Category: Chen Y]]
[[Category: Cheng, X]]
[[Category: Cheng X]]
[[Category: Huang, Y]]
[[Category: Huang Y]]
[[Category: Liu, N]]
[[Category: Liu N]]
[[Category: Lu, M]]
[[Category: Lu M]]
[[Category: White, M A]]
[[Category: White MA]]
[[Category: Wu, X]]
[[Category: Wu X]]
[[Category: Nadh]]
[[Category: Oxidoreductase]]

Latest revision as of 11:49, 20 March 2024

Substrate-directed dual catalysis of dicarbonyl compounds by diketoreductaseSubstrate-directed dual catalysis of dicarbonyl compounds by diketoreductase

Structural highlights

4dyd is a 1 chain structure with sequence from Acinetobacter baylyi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.95Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

B1P3E1_ACIBI

4dyd, resolution 1.95Å

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OCA
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