Fig. 6: Comparative molecular dynamics analysis of wild-type CYP204A5 and its variants (S91M, T323L, M324I) in complex with docked substrate CHO. | Nature Communications

Fig. 6: Comparative molecular dynamics analysis of wild-type CYP204A5 and its variants (S91M, T323L, M324I) in complex with docked substrate CHO.

From: Unveiling cytochrome P450 enzymes that catalyze steroid side-chain cleavage in bacteria

Fig. 6: Comparative molecular dynamics analysis of wild-type CYP204A5 and its variants (S91M, T323L, M324I) in complex with docked substrate CHO.

d1: the distance of Fe-O and C20; d2: the distance of Fe-O and C22. a A representative snapshot of CYP204A5-S91M with substrate CHO. b Statistics of the distance d1 and d2 for CYP204A5 and CYP204A5-S91M. c A representative snapshot of CYP204A5- T323L with substrate CHO. d Comparative statistics of distances d1 and d2 for CYP204A5 and CYP204A5-T323L. e A representative snapshot of CYP204A5-M324I with substrate CHO. f Comparative statistics of the distance d1 and d2 for CYP204A5 and CYP204A5-M324I.

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