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1d4e

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==CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE==
==CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE==
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<StructureSection load='1d4e' size='340' side='right' caption='[[1d4e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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<StructureSection load='1d4e' size='340' side='right'caption='[[1d4e]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1d4e]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Shewanella_oneidensis Shewanella oneidensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4E OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1D4E FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1d4e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Shewanella_oneidensis Shewanella oneidensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D4E FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2.8&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d4c|1d4c]], [[1d4d|1d4d]]</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=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEC:HEME+C'>HEC</scene></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'>[https://proteopedia.org/fgij/fg.htm?mol=1d4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4e OCA], [https://pdbe.org/1d4e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1d4e RCSB], [https://www.ebi.ac.uk/pdbsum/1d4e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1d4e ProSAT]</span></td></tr>
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<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=1d4e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d4e OCA], [http://pdbe.org/1d4e PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1d4e RCSB], [http://www.ebi.ac.uk/pdbsum/1d4e PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1d4e ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/FRDA_SHEON FRDA_SHEON]] 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).
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[https://www.uniprot.org/uniprot/FRDA_SHEON FRDA_SHEON] 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).
== 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: Large Structures]]
[[Category: Shewanella oneidensis]]
[[Category: Shewanella oneidensis]]
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[[Category: Succinate dehydrogenase]]
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[[Category: Cusanovich MA]]
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[[Category: Beeumen, J J.Van]]
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[[Category: Leys D]]
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[[Category: Cusanovich, M A]]
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[[Category: Meyer TE]]
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[[Category: Leys, D]]
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[[Category: Tsapin AS]]
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[[Category: Meyer, T E]]
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[[Category: Van Beeumen JJ]]
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[[Category: Tsapin, A S]]
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[[Category: Oxidoreductase]]
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[[Category: Tetraheme flavocytochrome c fumarate reductase]]
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Current revision

CRYSTAL STRUCTURE OF THE FLAVOCYTOCHROME C FUMARATE REDUCTASE OF SHEWANELLA PUTREFACIENS STRAIN MR-1 COMPLEXED WITH FUMARATE

PDB ID 1d4e

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