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==WrbA in complex with FMN under crystallization conditions of WrbA-FMN-BQ structure (4YQE)==
==WrbA in complex with FMN under crystallization conditions of WrbA-FMN-BQ structure (4YQE)==
<StructureSection load='5f12' size='340' side='right' caption='[[5f12]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='5f12' size='340' side='right'caption='[[5f12]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5f12]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F12 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5F12 FirstGlance]. <br>
<table><tr><td colspan='2'>[[5f12]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5F12 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5F12 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>, <scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4yqe|4yqe]], [[1rg1|1rg1]], [[3zho|3zho]]</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=5f12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f12 OCA], [https://pdbe.org/5f12 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5f12 RCSB], [https://www.ebi.ac.uk/pdbsum/5f12 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5f12 ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/NAD(P)H_dehydrogenase_(quinone) NAD(P)H dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.5.2 1.6.5.2] </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=5f12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5f12 OCA], [http://pdbe.org/5f12 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5f12 RCSB], [http://www.ebi.ac.uk/pdbsum/5f12 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5f12 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/NQOR_ECOLI NQOR_ECOLI]] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.<ref>PMID:16672604</ref> <ref>PMID:9694845</ref>
[https://www.uniprot.org/uniprot/NQOR_ECOLI NQOR_ECOLI] It seems to function in response to environmental stress when various electron transfer chains are affected or when the environment is highly oxidizing. It reduces quinones to the hydroquinone state to prevent interaction of the semiquinone with O2 and production of superoxide. It prefers NADH over NADPH.<ref>PMID:16672604</ref> <ref>PMID:9694845</ref>  
<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: Brynda, J]]
[[Category: Escherichia coli K-12]]
[[Category: Carey, J]]
[[Category: Large Structures]]
[[Category: Degtjarik, O]]
[[Category: Brynda J]]
[[Category: Ettrich, R]]
[[Category: Carey J]]
[[Category: Ettrichova, O]]
[[Category: Degtjarik O]]
[[Category: Smatanova, I Kuta]]
[[Category: Ettrich R]]
[[Category: Flavin mononucleotide]]
[[Category: Ettrichova O]]
[[Category: Oxidation-reduction]]
[[Category: Kuta Smatanova I]]
[[Category: Oxidoreductase]]
[[Category: Protein binding]]
[[Category: Repressor protein]]
Retrieved from "https://proteopedia.org/5f12"