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. Author manuscript; available in PMC: 2015 Jul 1.
Published in final edited form as: Biochemistry. 2013 Apr 11;52(16):2705–2707. doi: 10.1021/bi400280z

Figure 3.

Figure 3

View of the heme-binding pocket in the superimposed structures of apo-HasAyp tet and holo-HasAyp illustrate the minor structural differences between apo-(magenta) and holo-(green) HasAyp. The distal site in the holo protein is coordinated by a chloride ion; the Fo-Fc omit map contoured at 3 σ is shown in mesh representation.