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Bioresources and Bioprocessing
Fig. 4 | Bioresources and Bioprocessing

Fig. 4

From: Bacterial cytochrome P450-catalyzed regio- and stereoselective steroid hydroxylation enabled by directed evolution and rational design

Fig. 4

Active-site residues in the X-ray crystal structure of the N-palmitoylglycine (NPG)-bound form of the heme domain of wild-type P450BM3 (1JPZ). The nine sites are labeled as a (R47/T49/Y51), b (V78/A82), c (M185/L188), d (S72/A74/L75), e (L181/A184), f (T260/I263), g (A328/A330), h (L437, T438) and i (V26, L29). The mutant F87A is served as the starting template (Kille et al. 2011)

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