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Cytochrome P-450

This page shows some interactive JSmol views of several forms of cytochrome P-450


The first figure, [P450] shows the structure of a bacterial P-450. It is a heme protein with a cysteine sulfur coordinated to the iron in the heme active site. In this form the iron is low spin Fe(III) and the Fe-OH2 distance is 2.16 Å. Note there is quite good access to this site and a vacant space near the heme.

[P450/camphor] shows the P-450 from the same bacterium with camphor in the active site. The camphor is held in place by interactions with the protein. In some forms, P-450 binds one particular substrate molecule, in other cases it is less specific.

[P450/nicotine] shows a human P-450 with nicotine in the substrate site. The bound water molecule is displaced and the iron has been reduced to Fe(II), ready to react with 3O2.

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Written by V. McKee based on template by A. Herráez as modified by J. Gutow.
Page skeleton and JavaScript generated by export to web function using Jmol 14.2.15_2015.07.09 2015-07-09 22:22 updated November 2019.
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P-450 from Novosphingobium aromaticivorans with/without capmhor data from: The structure of CYP101D2 unveils a potential path for substrate entry into the active site. Yang, W., Bell, S.G., Wang, H., Zhou, W., Bartlam, M., Wong, L.L., Rao, Z. (2011) Biochem.J. 433: 85-93 (PDB code 3NV5 & 3NV6).
Human P-450 2A6 with Nicotine data from: Nicotine and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone binding and access channel in human cytochrome P450 2A6 and 2A13 enzymes. DeVore, N.M., Scott, E.E. (2012) J.Biol.Chem. 287: 26576-26585 (PDB code 4EJJ).

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