Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein–ligand interactions based on crystal structures of the ligand-bound enzyme
Version of Record online: 25 NOV 2011
© 2011 The Authors Journal compilation © 2011 FEBS
The FEBS Journal
Special Issue: Cytochrome P450 Structure and Function
Volume 279, Issue 9, pages 1607–1620, May 2012
How to Cite
Wilderman, P. R., Gay, S. C., Jang, H.-H., Zhang, Q., Stout, C. D. and Halpert, J. R. (2012), Investigation by site-directed mutagenesis of the role of cytochrome P450 2B4 non-active-site residues in protein–ligand interactions based on crystal structures of the ligand-bound enzyme. The FEBS Journal, 279: 1607–1620. doi: 10.1111/j.1742-4658.2011.08411.x
- Issue online: 19 APR 2012
- Version of Record online: 25 NOV 2011
- Accepted manuscript online: 3 NOV 2011 01:34PM EST
- (Received 7 September 2011, revised 17 October 2011, accepted 21 October 2011)
Fig. S1. Variation in distance between closest non-hydrogen atoms in PDB structures for each interaction. The average distance between interaction partners as measured by g_mindist.
Table S1. Oligonucleotides used for site-directed mutagenesis of 2B4 using PCR.
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