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. Author manuscript; available in PMC: 2011 May 30.
Published in final edited form as: J Med Chem. 2009 Apr 9;52(7):2060–2066. doi: 10.1021/jm900007a

Fig. 4.

Fig. 4

Active site structures of the wild type eNOS with inhibitor 6 (panel A) or 7 (panel B) bound. Also shown around the inhibitor is the Fo – Fc omit map contoured at 3.0σ. Residue Trp76 belongs to the neighboring subunit. Alternate conformations of heme propionate off the pyrrole ring D are also depicted.