3vr8: Difference between revisions

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 ==Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum==
-<StructureSection load='3vr8' size='340' side='right' caption='[[3vr8]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
+<StructureSection load='3vr8' size='340' side='right'caption='[[3vr8]], [[Resolution|resolution]] 2.81&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3vr8]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VR8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VR8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3vr8]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Ascaris_suum Ascaris suum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VR8 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</scene>, <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=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=RQX:2-AMINO-3-METHOXY-6-METHYL-5-[(2E)-3-METHYLHEX-2-EN-1-YL]CYCLOHEXA-2,5-DIENE-1,4-DIONE'>RQX</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]] 2.81&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vrb|3vrb]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPH:L-ALPHA-PHOSPHATIDYL-BETA-OLEOYL-GAMMA-PALMITOYL-PHOSPHATIDYLETHANOLAMINE'>EPH</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=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=RQX:2-AMINO-3-METHOXY-6-METHYL-5-[(2E)-3-METHYLHEX-2-EN-1-YL]CYCLOHEXA-2,5-DIENE-1,4-DIONE'>RQX</scene></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=3vr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vr8 OCA], [http://pdbe.org/3vr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3vr8 RCSB], [http://www.ebi.ac.uk/pdbsum/3vr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3vr8 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=3vr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vr8 OCA], [https://pdbe.org/3vr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vr8 RCSB], [https://www.ebi.ac.uk/pdbsum/3vr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vr8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DHSD_ASCSU DHSD_ASCSU]] Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity).
+[https://www.uniprot.org/uniprot/SDHA1_ASCSU SDHA1_ASCSU] Flavoprotein (Fp) subunit of the mitochondrial electron transport chain complex II which, together with the iron-sulfur protein (Ip) subunit forms the catalytic core of the complex (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436). During the parasitic larvae and adult stages, which occur in an anaerobic environment, acts as a fumarate reductase by transferring electrons from rhodoquinol to fumarate (PubMed:12742584, PubMed:17933581, PubMed:2843227, PubMed:7739664, PubMed:7822332, PubMed:8435436).<ref>PMID:12742584</ref> <ref>PMID:17933581</ref> <ref>PMID:2843227</ref> <ref>PMID:7739664</ref> <ref>PMID:7822332</ref> <ref>PMID:8435436</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 3vr8" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
 == References ==
 <references/>
@@ Line 24: / Line 27: @@
 </StructureSection>
 [[Category: Ascaris suum]]
-[[Category: Harada, S]]
+[[Category: Large Structures]]
-[[Category: Inaoka, D K]]
+[[Category: Harada S]]
-[[Category: Kita, K]]
+[[Category: Inaoka DK]]
-[[Category: Osanai, A]]
+[[Category: Kita K]]
-[[Category: Sakamoto, K]]
+[[Category: Osanai A]]
-[[Category: Shiba, T]]
+[[Category: Sakamoto K]]
-[[Category: Shimizu, H]]
+[[Category: Shiba T]]
-[[Category: Membrane protein]]
+[[Category: Shimizu H]]
-[[Category: Mitochondria membrane]]
-[[Category: Oxidoreductase]]
-[[Category: Reductase]]