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==Crystal structure of porcine heart mitochondrial complex II bound with 2-Methyl-N-(3-isopropoxy-phenyl)-benzamide==
==Crystal structure of porcine heart mitochondrial complex II bound with 2-Methyl-N-(3-isopropoxy-phenyl)-benzamide==
<StructureSection load='3ae5' size='340' side='right' caption='[[3ae5]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
<StructureSection load='3ae5' size='340' side='right' caption='[[3ae5]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
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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=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene>, <scene name='pdbligand=MRN:2-METHYL-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE'>MRN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
</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=MRN:2-METHYL-N-[3-(1-METHYLETHOXY)PHENYL]BENZAMIDE'>MRN</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3ae9|3ae9]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aec|3aec]], [[3aed|3aed]], [[3aee|3aee]], [[3aef|3aef]], [[3aeg|3aeg]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3abv|3abv]], [[3ae1|3ae1]], [[3ae2|3ae2]], [[3ae3|3ae3]], [[3ae4|3ae4]], [[3ae6|3ae6]], [[3ae7|3ae7]], [[3ae8|3ae8]], [[3ae9|3ae9]], [[3aea|3aea]], [[3aeb|3aeb]], [[3aec|3aec]], [[3aed|3aed]], [[3aee|3aee]], [[3aef|3aef]], [[3aeg|3aeg]]</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_(ubiquinone) Succinate dehydrogenase (ubiquinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </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_(quinone) Succinate dehydrogenase (quinone)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.5.1 1.3.5.1] </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=3ae5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ae5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ae5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ae5 PDBsum]</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=3ae5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ae5 OCA], [http://pdbe.org/3ae5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ae5 RCSB], [http://www.ebi.ac.uk/pdbsum/3ae5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ae5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/DHSD_PIG DHSD_PIG]] 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). [[http://www.uniprot.org/uniprot/DHSA_PIG DHSA_PIG]] Flavoprotein (FP) 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). Can act as a tumor suppressor (By similarity). [[http://www.uniprot.org/uniprot/C560_PIG C560_PIG]] 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).<ref>PMID:17480203</ref>  [[http://www.uniprot.org/uniprot/DHSB_PIG DHSB_PIG]] Iron-sulfur protein (IP) 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).  
[[http://www.uniprot.org/uniprot/DHSD_PIG DHSD_PIG]] 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). [[http://www.uniprot.org/uniprot/SDHA_PIG SDHA_PIG]] Flavoprotein (FP) 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). Can act as a tumor suppressor (By similarity). [[http://www.uniprot.org/uniprot/C560_PIG C560_PIG]] 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).<ref>PMID:17480203</ref>  [[http://www.uniprot.org/uniprot/SDHB_PIG SDHB_PIG]] Iron-sulfur protein (IP) 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).  


==See Also==
==See Also==

Revision as of 17:50, 5 August 2016

Crystal structure of porcine heart mitochondrial complex II bound with 2-Methyl-N-(3-isopropoxy-phenyl)-benzamideCrystal structure of porcine heart mitochondrial complex II bound with 2-Methyl-N-(3-isopropoxy-phenyl)-benzamide

Structural highlights

3ae5 is a 4 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , , , , , ,
Activity:Succinate dehydrogenase (quinone), with EC number 1.3.5.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DHSD_PIG] 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). [SDHA_PIG] Flavoprotein (FP) 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). Can act as a tumor suppressor (By similarity). [C560_PIG] 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).[1] [SDHB_PIG] Iron-sulfur protein (IP) 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).

See Also

References

  1. ↑ Huo X, Su D, Wang A, Zhai Y, Xu J, Li X, Bartlam M, Sun F, Rao Z. Preliminary molecular characterization and crystallization of mitochondrial respiratory complex II from porcine heart. FEBS J. 2007 Mar;274(6):1524-9. PMID:17480203 doi:http://dx.doi.org/10.1111/j.1742-4658.2007.05698.x

3ae5, resolution 3.41Å

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