Cytochromes P450 comprise a very large superfamily of hemeproteins which generally monooxygenate hydrophobic compounds. P450s appear to have a common conserved structural core, yet are variable in regions involved in substrate recognition and binding, and in redox-partner binding. These differences can be identified by an analysis in which structural alignments and homology models are used to compare the various classes and families of P450s.
Peterson, J. A., & Graham, S. E. (1998). A close family resemblance: The importance of structure in understanding cytochromes P450. Structure, 6(9), 1079–1085. https://doi.org/10.1016/S0969-2126(98)00109-9