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1y0p

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Current revision (08:09, 25 October 2023) (edit) (undo)
 
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<StructureSection load='1y0p' size='340' side='right'caption='[[1y0p]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='1y0p' size='340' side='right'caption='[[1y0p]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1y0p]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Acam_591 Acam 591]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1Y0P FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1y0p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_frigidimarina Shewanella frigidimarina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y0P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Y0P 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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MEZ:(2E)-2-METHYLBUT-2-ENEDIOIC+ACID'>MEZ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.5&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qjd|1qjd]]</div></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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MEZ:(2E)-2-METHYLBUT-2-ENEDIOIC+ACID'>MEZ</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fccA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56812 ACAM 591])</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=1y0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0p OCA], [https://pdbe.org/1y0p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1y0p RCSB], [https://www.ebi.ac.uk/pdbsum/1y0p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0p ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1y0p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1y0p OCA], [http://pdbe.org/1y0p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1y0p RCSB], [http://www.ebi.ac.uk/pdbsum/1y0p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1y0p ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FRDA_SHEFR FRDA_SHEFR]] Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional.
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[https://www.uniprot.org/uniprot/FRDA_SHEFR FRDA_SHEFR] Catalyzes fumarate reduction using artificial electron donors such as methyl viologen. The physiological reductant is unknown, but evidence indicates that flavocytochrome c participates in electron transfer from formate to fumarate and possibly also to trimethylamine oxide (TMAO). This enzyme is essentially unidirectional.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acam 591]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Succinate dehydrogenase]]
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[[Category: Shewanella frigidimarina]]
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[[Category: Chapman, S K]]
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[[Category: Chapman SK]]
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[[Category: Mowat, C G]]
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[[Category: Mowat CG]]
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[[Category: Reid, G A]]
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[[Category: Reid GA]]
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[[Category: Wardrope, C]]
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[[Category: Wardrope C]]
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[[Category: Flavocytochrome]]
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[[Category: Fumarate reductase]]
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[[Category: Mesaconate]]
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[[Category: Oxidoreductase]]
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Current revision

Flavocytochrome c3 with mesaconate bound

PDB ID 1y0p

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