1lj1: Difference between revisions

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<StructureSection load='1lj1' size='340' side='right'caption='[[1lj1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='1lj1' size='340' side='right'caption='[[1lj1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1lj1]] is a 2 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=1LJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJ1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[1lj1]] is a 2 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=1LJ1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LJ1 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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</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]] 2&#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;'>[[1jrx|1jrx]], [[1jry|1jry]], [[1jrz|1jrz]], [[1kss|1kss]], [[1ksu|1ksu]], [[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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fcc ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56812 ACAM 591])</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=1lj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj1 OCA], [https://pdbe.org/1lj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lj1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lj1 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=1lj1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lj1 OCA], [https://pdbe.org/1lj1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lj1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lj1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lj1 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[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.  
[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>
[[Category: Acam 591]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Succinate dehydrogenase]]
[[Category: Shewanella frigidimarina]]
[[Category: Chapman, S K]]
[[Category: Chapman SK]]
[[Category: Leys, D]]
[[Category: Leys D]]
[[Category: Miles, C S]]
[[Category: Miles CS]]
[[Category: Mowat, C G]]
[[Category: Mowat CG]]
[[Category: Pankhurst, K L]]
[[Category: Pankhurst KL]]
[[Category: Reid, G A]]
[[Category: Reid GA]]
[[Category: Walkinshaw, M D]]
[[Category: Walkinshaw MD]]
[[Category: Flavocytochrome]]
[[Category: Fumarate reductase]]
[[Category: Oxidoreductase]]

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