Class I cytochrome P450 enzymes (CYPs) receive two electrons sequentially from NAD(P)H via a cognate ferredoxin reductase and ferredoxin, and are responsible for tasks as diverse as mitochondrial vitamin D3 hydroxylation and bacterial antibiotic synthesis. The interaction of these Class I CYPs with their cognate ferredoxin is specific and the first electron-transfer step is rate limiting. In order to reconstitute the activity of diverse CYPs, structural characterization of CYP:ferredoxin complexes is necessary, but little structural information is available. We report a rigid-body model of such a complex (CYP199A2:HaPux) in frozen solution derived from distance and orientation restraints gathered by orientation-dependent double electron-electron resonance (DEER), an EPR technique.