1. The construction of three-dimensional models of mammalian cytochrom
es P450 from the CYP2 family is reported based on protein sequence ali
gnment with CYP102, a bacterial P450 of known crystal structure. 2. Th
e homology models of CYP2 family enzymes appear to show self-consisten
cy with the currently accumulated information from site-directed mutag
enesis and chemical modification of amino acid residues known to affec
t redox partner interactions. 3. The generation of these models from t
he recently reported crystal structure of substrate-bound CYP102 enabl
es the exploration of likely active site contacts with specific substr
ates of CYP2 family isozymes.