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<StructureSection load='1e39' size='340' side='right'caption='[[1e39]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1e39' size='340' side='right'caption='[[1e39]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1e39]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acam_591 Acam 591]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E39 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1e39]] 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=1E39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E39 FirstGlance]. <br>
</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=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.8&#8491;</td></tr>
<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>
<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=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Succinate_dehydrogenase Succinate dehydrogenase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.1 1.3.99.1] </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=1e39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e39 OCA], [https://pdbe.org/1e39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e39 RCSB], [https://www.ebi.ac.uk/pdbsum/1e39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e39 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=1e39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e39 OCA], [https://pdbe.org/1e39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e39 RCSB], [https://www.ebi.ac.uk/pdbsum/1e39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e39 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/FRDA_SHEFN FRDA_SHEFN]] 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 (By similarity).  
[https://www.uniprot.org/uniprot/FCCA_SHEFR FCCA_SHEFR] Flavocytochrome that catalyzes the reduction of fumarate to succinate (PubMed:10978153). Is essential for fumarate respiration during anaerobic growth, acting as the terminal reductase (By similarity). Receives electrons from the membrane-bound tetraheme c-type cytochrome CymA (By similarity). In vitro, can use the artificial electron donor methyl viologen (PubMed:10978153).[UniProtKB:P83223][UniProtKB:Q07WU7]<ref>PMID:10978153</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e39_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e3/1e39_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Acam 591]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Succinate dehydrogenase]]
[[Category: Shewanella frigidimarina]]
[[Category: Chapman, S K]]
[[Category: Chapman SK]]
[[Category: Doherty, M K]]
[[Category: Doherty MK]]
[[Category: Miles, C S]]
[[Category: Miles CS]]
[[Category: Moysey, R]]
[[Category: Moysey R]]
[[Category: Pealing, S L]]
[[Category: Pealing SL]]
[[Category: Reid, G A]]
[[Category: Reid GA]]
[[Category: Taylor, P]]
[[Category: Taylor P]]
[[Category: Walkinshaw, M D]]
[[Category: Walkinshaw MD]]
[[Category: Fumarate reductase mutant h365a]]
[[Category: Oxidoreductase]]
[[Category: Respiratory fumarate reductase]]

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