Fig. 6: X-ray crystal structure of QhpG. | Nature Communications

Fig. 6: X-ray crystal structure of QhpG.

From: Functional and structural characterization of a flavoprotein monooxygenase essential for biogenesis of tryptophylquinone cofactor

Fig. 6

a Overall structure of QhpG monomer. The monomer structure (chain A) is depicted by a cartoon model with a spherical model of the bound FAD. b Structure of FAD-binding site. A stick model of the bound FAD is shown with the surrounding residues. An FoFc omit map for FAD, contoured at 5σ, is depicted by blue mesh. Hydrogen bonds and water molecules are shown by yellow dotted lines and red small spheres, respectively. c, d Channels formed in the re-face (c) and si-face (d) sides of FAD (in chain B) is shown with stick models of the side chains (yellow) on the white cartoon model of QhpG. 1,6-Hexanediol (Hdol) and cyclohexyl-methyl-β-d-maltoside (Cymal-1) (additives in crystallization buffer) bound to the re-face channel are indicated by orange stick models. FAD is indicated by a spherical model.

Back to article page