Fig. 5: Crystal structure of the CYP204A3 and structure-guided mutagenesis analysis of critical residues in bacterial P450scc.
From: Unveiling cytochrome P450 enzymes that catalyze steroid side-chain cleavage in bacteria
a The overall structures of CYP204A3. b Docking structure of CHO (cyan) with CYP204A3 (light pink) and residues around substrate-binding pocket within 5 Å. The blue color highlights the corresponding amino acid residues of CYP204A5. The distances between heme-Fe of CYP204A3 and C20/22 of CHO are indicated with yellow dash lines. c The distance from iron-oxo species to C20 (light pink) and C22 (cyan) of CHO over the course of a 100 nanosecond MD simulation for CYP204A3. d WebLogo of the residues around substrate-pocket with 5 Å for several bacteria-derived P450sccs (CYP204 A2-A6, CYP204B2). e The relative activity of CYP204A3 and its mutants in catalyzing the generation of PROG from CHO. All data points were obtained in three replicate experiments. Data are presented as the mean ± SEM unless otherwise noted. ND: not detected. f The relative activity of CYP204A5 and its mutants in catalyzing the generation of PROG from CHO. All data points were obtained in three replicate experiments. Data are presented as the mean ± SEM unless otherwise noted. Source data are provided as a Source Data file.
