1.8.5.8	coenzyme Q	-	764977, 765845	
1.8.5.8	coenzyme Q10	CoQ10	764431	
1.8.5.8	decylubiquinone	-	764408, 764431	
1.8.5.8	FAD	-	742905, 744311, 745263	
1.8.5.8	FAD	required	764431, 764484, 764977	
1.8.5.8	FAD	required, FAD is noncovalently bound in an extended conformation and is in the oxidized state. The first Rossmann fold starts near the N-terminus and binds the ADP portion of FAD. The second Rossmann fold is closer to the isoalloxazine ring of FAD but is mostly positioned at least 10 A away from the flavin ring with one notable exception. FAD is bound in an extended conformation. Its interactions with the protein include 12 hydrogen bonds and electrostatic interactions with two helix dipoles. Two basic residues, Lys207 and Lys418, lie above the flavin's re- and si-face, respectively with their respective epsilon-amino groups 3.2 and 3.3 A from a carbonyl oxygen in the isoalloxazine ring (O4). Binding site structure, overview	765845	
1.8.5.8	FAD	the deduced ScSQR protein contains conserved FAD-binding domains, comprising residues 32-59, 121-134, and 306-331	764525	
1.8.5.8	additional information	molecular dynamics simulations and QM/MM reactivity predictors for a disulfide versus trisulfide cofactor involving FAD, overview	764977	
1.8.5.8	ubiquinone	-	764525