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. Author manuscript; available in PMC: 2008 Jun 23.
Published in final edited form as: J Am Chem Soc. 2003 Nov 12;125(45):13804–13818. doi: 10.1021/ja035654x

Figure 1.

Figure 1

Crystal structure of MbCO taken from the Protein Data Bank (1A6G). The heme group and three residues are indicated explicitly. The heme iron is covalently bound to the protein via His93. His64 is thought to play a major role in the conformational substates of the protein. Secondary structure is color-coded: helix A, blue; helix B, red; helix C, purple; helix D, green; helix E, orange; helix F, brown; helix G, pink; helix H, gray. All loops are colored cyan.