Skip to main content
. Author manuscript; available in PMC: 2019 Apr 17.
Published in final edited form as: Biochemistry. 2018 Jan 26;57(6):963–977. doi: 10.1021/acs.biochem.7b01137

Figure 4.

Figure 4.

Comparison of the cofactor-binding environment in SmGhrA and SmGhrB. (A, C) Residues forming hydrogen bonds with the cofactor. (B, D) 2′-Phosphate binding site formed by the S(T)RS(T)XR(K) motif (nonconserved residue X is not shown). The cofactor is shown in stick representation; oxygen atoms are depicted in red, carbon in green, nitrogen in blue, and phosphorus in orange. Amino acid residues involved in the cofactor binding by hydrogen bonding are shown in a similar color schema with carbon depicted in gray. Hydrogen bonds are indicated as red dashed lines. Residues from the coenzyme-binding domain are labeled in black, and residues from the catalytic domain are labeled in magenta.