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Results 1 - 9 of 9
EC Number Cofactor Commentary Reference
Display the reaction diagram Show all sequences 1.8.5.8coenzyme Q - 764977, 765845
Display the reaction diagram Show all sequences 1.8.5.8coenzyme Q10 CoQ10 764431
Display the reaction diagram Show all sequences 1.8.5.8decylubiquinone - 764408, 764431
Display the reaction diagram Show all sequences 1.8.5.8FAD - 742905, 744311, 745263
Display the reaction diagram Show all sequences 1.8.5.8FAD required 764431, 764484, 764977
Display the reaction diagram Show all sequences 1.8.5.8FAD 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
Display the reaction diagram Show all sequences 1.8.5.8FAD the deduced ScSQR protein contains conserved FAD-binding domains, comprising residues 32-59, 121-134, and 306-331 764525
Display the reaction diagram Show all sequences 1.8.5.8more molecular dynamics simulations and QM/MM reactivity predictors for a disulfide versus trisulfide cofactor involving FAD, overview 764977
Display the reaction diagram Show all sequences 1.8.5.8ubiquinone - 764525
Results 1 - 9 of 9