1ksu: Difference between revisions

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 ==Crystal Structure of His505Tyr Mutant Flavocytochrome c3 from Shewanella frigidimarina==
-<StructureSection load='1ksu' size='340' side='right' caption='[[1ksu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='1ksu' size='340' side='right'caption='[[1ksu]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ksu]] is a 2 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=1KSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KSU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ksu]] 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=1KSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KSU FirstGlance]. <br>
-</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>, <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">[[1jrx|1jrx]], [[1jry|1jry]], [[1jrz|1jrz]], [[1e39|1e39]], [[1qjd|1qjd]], [[1kss|1kss]]</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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=56812 ACAM 591])</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=1ksu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksu OCA], [https://pdbe.org/1ksu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ksu RCSB], [https://www.ebi.ac.uk/pdbsum/1ksu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksu 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/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>
-<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=1ksu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ksu OCA], [http://pdbe.org/1ksu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ksu RCSB], [http://www.ebi.ac.uk/pdbsum/1ksu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ksu ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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.
+[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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 29: @@
 </div>
 <div class="pdbe-citations 1ksu" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Flavocytochrome 3D structures|Flavocytochrome 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Acam 591]]
+[[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 c3]]
-[[Category: Fumarate reductase]]
-[[Category: H505y]]
-[[Category: Oxidoreductase]]