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3vrb

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==Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate==
==Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate==
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<StructureSection load='3vrb' size='340' side='right' caption='[[3vrb]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
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<StructureSection load='3vrb' size='340' side='right'caption='[[3vrb]], [[Resolution|resolution]] 2.91&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3vrb]] 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=3VRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3VRB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3vrb]] 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=3VRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VRB 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=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=FTN:N-[3-(1-METHYLETHOXY)PHENYL]-2-(TRIFLUOROMETHYL)BENZAMIDE'>FTN</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</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]] 2.91&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3vr8|3vr8]]</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=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=FTN:N-[3-(1-METHYLETHOXY)PHENYL]-2-(TRIFLUOROMETHYL)BENZAMIDE'>FTN</scene>, <scene name='pdbligand=FUM:FUMARIC+ACID'>FUM</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></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=3vrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vrb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3vrb RCSB], [http://www.ebi.ac.uk/pdbsum/3vrb PDBsum]</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=3vrb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vrb OCA], [https://pdbe.org/3vrb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vrb RCSB], [https://www.ebi.ac.uk/pdbsum/3vrb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vrb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[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).
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[https://www.uniprot.org/uniprot/Q33862_ASCSU Q33862_ASCSU]
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
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<div class="pdbe-citations 3vrb" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
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*[[Succinate Dehydrogenase|Succinate Dehydrogenase]]
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*[[Succinate dehydrogenase 3D structures|Succinate dehydrogenase 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
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[[Category: Harada, S]]
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[[Category: Large Structures]]
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[[Category: Inaoka, D K]]
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[[Category: Harada S]]
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[[Category: Kita, K]]
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[[Category: Inaoka DK]]
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[[Category: Osanai, A]]
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[[Category: Kita K]]
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[[Category: Sakamoto, K]]
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[[Category: Osanai A]]
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[[Category: Shiba, T]]
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[[Category: Sakamoto K]]
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[[Category: Shimizu, H]]
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[[Category: Shiba T]]
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[[Category: Membrane protein]]
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[[Category: Shimizu H]]
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[[Category: Mitochondrial membrane]]
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[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
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[[Category: Reductase]]
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Current revision

Mitochondrial rhodoquinol-fumarate reductase from the parasitic nematode Ascaris suum with the specific inhibitor flutolanil and substrate fumarate

PDB ID 3vrb

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