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Figure 1
Crystal structure of the Qi site of bovine bc1 with the SCR0911 inhibitor bound. (a) Cartoon representation of cytochrome b (blue) and the Rieske protein (grey). The Qo and Qi sites of the cytochrome b subunit are highlighted in black boxes. Haems bL and bH are shown as blue sticks. Omit Fo − Fc electron density (in green) is contoured at the 3σ level, showing density for the SCR0911 inhibitor. (b) SCR0911 inhibitor bound in the Qi site. Residues and inhibitor are shown as sticks. The 2Fo − Fc electron-density map is contoured at the 1σ level, with the inhibitor density coloured green and the protein density in purple. Hydrogen bonds between inhibitors and residues are illustrated by black dashed lines. (c) The crystal structures of the Qi site in bc1–SCR0911 (purple) and bc1–GSK932121 (grey) have been superimposed, showing the different binding modes of the pyridone (GSK932121, grey) and quinolone (SCR0911, purple) inhibitors.

IUCrJ
Volume 5| Part 2| March 2018| Pages 200-210
ISSN: 2052-2525
https://doi.org/10.1107/S2052252518001616