5c3j: Difference between revisions

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<StructureSection load='5c3j' size='340' side='right'caption='[[5c3j]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
<StructureSection load='5c3j' size='340' side='right'caption='[[5c3j]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5c3j]] 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=5C3J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C3J FirstGlance]. <br>
<table><tr><td colspan='2'>[[5c3j]] 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=5C3J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C3J 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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene></td></tr>
</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=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=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=UQ1:UBIQUINONE-1'>UQ1</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c2t|5c2t]]</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=5c3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3j OCA], [https://pdbe.org/5c3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c3j RCSB], [https://www.ebi.ac.uk/pdbsum/5c3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c3j 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_(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=5c3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c3j OCA], [http://pdbe.org/5c3j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c3j RCSB], [http://www.ebi.ac.uk/pdbsum/5c3j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c3j ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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). [[http://www.uniprot.org/uniprot/U1LRQ3_ASCSU U1LRQ3_ASCSU]] 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).[RuleBase:RU362051]  
[https://www.uniprot.org/uniprot/Q33862_ASCSU Q33862_ASCSU]  


==See Also==
==See Also==
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[[Category: Ascaris suum]]
[[Category: Ascaris suum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Harada, S]]
[[Category: Harada S]]
[[Category: Honma, T]]
[[Category: Honma T]]
[[Category: Inaoka, D K]]
[[Category: Inaoka DK]]
[[Category: Inoue, M]]
[[Category: Inoue M]]
[[Category: Kita, K]]
[[Category: Kita K]]
[[Category: Nagahama, M]]
[[Category: Nagahama M]]
[[Category: Sakamoto, K]]
[[Category: Sakamoto K]]
[[Category: Sato, D]]
[[Category: Sato D]]
[[Category: Shiba, T]]
[[Category: Shiba T]]
[[Category: Yamamoto, A]]
[[Category: Yamamoto A]]
[[Category: Yone, A]]
[[Category: Yone A]]
[[Category: Complex ii]]
[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
[[Category: Rhodoquinol-fumarate reductase]]

Revision as of 06:18, 7 June 2023

Crystal structure of Mitochondrial rhodoquinol-fumarate reductase from Ascaris suum with Ubiquinone-1

5c3j, resolution 2.80Å

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