cover illustration Cytochrome P450 monooxygenease (P450s) represent an important class of proteins found across the evolutionary tree with a limited amount of experimental structures. Structural and functional modeling of P450s from knowledge of their sequence is particularly desirable but is made difficult by the high sequence diversity among all P450s.The article by Baudry, Rupasinghe and Schuler (see pages 345–353) shows that the quality of P450 homology models is significantly improved by modeling strategies that discriminate P450s according to their electron transfer partners and use different templates for modeling of structurally conserved versus variable regions. Improved structural models translate into improved predictions of ligand binding geometries.
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