1e7p: Difference between revisions

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 <StructureSection load='1e7p' size='340' side='right'caption='[[1e7p]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1e7p]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_29543 Atcc 29543]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7P OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1E7P FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1e7p]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Wolinella_succinogenes Wolinella succinogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E7P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E7P FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 3.1&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">frdA, WS0831 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=844 ATCC 29543]), frdB, WS0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=844 ATCC 29543]), frdC, WS0832 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=844 ATCC 29543])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=F3S:FE3-S4+CLUSTER'>F3S</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Fumarate_reductase_(quinol) Fumarate reductase (quinol)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.4 1.3.5.4] </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=1e7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7p OCA], [https://pdbe.org/1e7p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e7p RCSB], [https://www.ebi.ac.uk/pdbsum/1e7p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7p ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1e7p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e7p OCA], [http://pdbe.org/1e7p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e7p RCSB], [http://www.ebi.ac.uk/pdbsum/1e7p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e7p ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FRDA_WOLSU FRDA_WOLSU]] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [[http://www.uniprot.org/uniprot/FRDC_WOLSU FRDC_WOLSU]] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor. [[http://www.uniprot.org/uniprot/FRDB_WOLSU FRDB_WOLSU]] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
+[https://www.uniprot.org/uniprot/FRDA_WOLSU FRDA_WOLSU] The fumarate reductase enzyme complex is required for fumarate respiration using formate or sulfide as electron donor.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 __TOC__
 </StructureSection>
-[[Category: Atcc 29543]]
 [[Category: Large Structures]]
-[[Category: Kroeger, A]]
+[[Category: Wolinella succinogenes]]
-[[Category: Lancaster, C R.D]]
+[[Category: Kroeger A]]
-[[Category: Citric acid cycle]]
+[[Category: Lancaster CRD]]
-[[Category: Dihaem cytochrome b]]
-[[Category: Flavoprotein]]
-[[Category: Iron- sulphur protein iron- sulphur protein]]
-[[Category: Oxidoreductase]]
-[[Category: Respiratory chain]]
-[[Category: Succinate dehydrogenase]]