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. Author manuscript; available in PMC: 2014 Aug 11.
Published in final edited form as: Nucleosides Nucleotides Nucleic Acids. 2009 May;28(5):485–503. doi: 10.1080/15257770903051031

Figure 2.

Figure 2

Open conformation (pdb: 1KY4, rat source) and closed conformation (pdb: 1LI4, human source) of the SAHH monomer (created by Molecular Operation Environment). The top domain is the cofactor-binding domain; the bottom domain is the substrate-binding domain; the loop at the right is the C-terminal extension. SAHH in the open conformation contains cofactor NAD+ (ball-and-stick) and SAHH in closed conformation contains cofactor NADH (ball-and-stick) and oxidized inhibitor-NepA (ball-and-stick). From the open conformation, the substrate-binding domain rotates ~ 19° toward to the cofactor binding domain to form an active site for catalysis in the closed conformation.