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2ACZ

Complex II (Succinate Dehydrogenase) From E. Coli with Atpenin A5 inhibitor co-crystallized at the ubiquinone binding site

Summary for 2ACZ
Entry DOI10.2210/pdb2acz/pdb
Related1NEK 1NEN 2AD0
DescriptorSuccinate dehydrogenase flavoprotein subunit, HEME B/C, 3-[(2S,4S,5R)-5,6-DICHLORO-2,4-DIMETHYL-1-OXOHEXYL]-4-HYDROXY-5,6-DIMETHOXY-2(1H)-PYRIDINONE, ... (12 entities in total)
Functional Keywordsmembrane protein, aerobic reparatory complex ii, sqr, succinate:ubiquinone oxidoreductase, aa5, at5, atpenin a5, sdh, succinate dehydrogenase, oxidoreductase-electron transport complex, oxidoreductase/electron transport
Biological sourceEscherichia coli
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Cellular locationCell inner membrane ; Peripheral membrane protein : P07014
Cell inner membrane; Multi-pass membrane protein: P69054
Total number of polymer chains4
Total formula weight122367.34
Authors
Horsefield, R.,Yankovskaya, V.,Sexton, G.,Whittingham, W.,Shiomi, K.,Omura, S.,Byrne, B.,Cecchini, G.,Iwata, S. (deposition date: 2005-07-19, release date: 2006-01-03, Last modification date: 2023-10-25)
Primary citationHorsefield, R.,Yankovskaya, V.,Sexton, G.,Whittingham, W.,Shiomi, K.,Omura, S.,Byrne, B.,Cecchini, G.,Iwata, S.
Structural and computational analysis of the quinone-binding site of complex II (succinate-ubiquinone oxidoreductase): a mechanism of electron transfer and proton conduction during ubiquinone reduction.
J.Biol.Chem., 281:7309-7316, 2006
Cited by
PubMed: 16407191
DOI: 10.1074/jbc.M508173200
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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