The active site of cytochrome P-450 nifedipine oxidase: a model-building study.
A model of the active site of cytochrome P-450 nifedipine oxidase is built on the basis of sequence homology with cytochrome P-450CAM. Substrates are docked into the binding pocket, and molecular mechanical energy minimization is performed to analyze the forces between the substrates and the enzyme.
Ferenczy
G G
GG
Physical Chemistry Laboratory, Oxford University, UK.
Morris
G M
GM
D001665:Binding Sites; D019475:Camphor 5-Monooxygenase; D003196:Computer Graphics; D051544:Cytochrome P-450 CYP3A; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008956:Models, Chemical; D009154:Mutation; D011802:Quinidine / Q000378:metabolism; D012689:Sequence Homology, Nucleic Acid; D013739:Testosterone / Q000378:metabolism
D013739:Testosterone; D003577:Cytochrome P-450 Enzyme System; D006899:Mixed Function Oxygenases; C104464:CYP3A protein, human; D051544:Cytochrome P-450 CYP3A; D019475:Camphor 5-Monooxygenase; D011802:Quinidine