Fig. 2: The structure of CcbD. | Nature Catalysis

Fig. 2: The structure of CcbD.

From: Molecular basis for carrier protein-dependent amide bond formation in the biosynthesis of lincosamide antibiotics

Fig. 2

a, The homodimer structure of CcbD. The α/β-fold domain, four anti-parallel β-sheets and C-terminal five α-helix domain are coloured green, magenta and cyan, respectively. b, The active site pocket of CcbD and the catalytic triad. c, The active site architecture and binding mode of substrate 8. Dashed yellow lines represent hydrogen bonds. Dashed cyan lines show distances between the amino group of 8 and catalytic residues. Water molecules are shown with red non-bonded spheres. d, Fo–Fc polder map of 8. The electron density maps of 8 (contoured at +3.0σ) in c and d are represented by a grey mesh. The catalytic residues are highlighted with red.

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