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
Article first published online: 25 NOV 2011
© 2011 The Authors Journal compilation © 2011 FEBS
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. FEBS Journal, 279: 1607–1620. doi: 10.1111/j.1742-4658.2011.08411.x
- Issue published online: 19 APR 2012
- Article first published 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.
Please note: As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer-reviewed and may be re-organized for online delivery, but are not copy-edited or typeset. Technical support issues arising from supporting information (other than missing files) should be addressed to the authors.
|FEBS_8411_sm_TableS1-FigS1.zip||737K||Supporting info item|
Please note: Wiley Blackwell is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.