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. Author manuscript; available in PMC: 2014 Feb 5.
Published in final edited form as: Biochemistry. 2013 Jan 24;52(5):902–911. doi: 10.1021/bi301652y

Figure 3.

Figure 3

The active site of LnmK. (A) Sigma weighted Fo-Fc omit map at 3 σ in green mesh depicting the phosphopantetheine moiety in the co-crystal structure of LnmK (Tyr62Phe) with methylmalonyl-CoA. (B) Tyrosine modeled into the co-crystal structure of LnmK (Tyr62Phe) with methylmalonyl-CoA showing the 2Fo-Fc map in blue at 1 σ and the Fo-Fc map at −3 σ in red. (C) Stereoview showing the amino acid side chains lining the active site tunnel from the co-crystal structure of LnmK with methylmalonyl-CoA. The bound chloride is shown as a purple sphere. Residues emanating from the crystallographic dimer are shown in gray.