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. Author manuscript; available in PMC: 2008 Oct 30.
Published in final edited form as: Biochemistry. 2008 Mar 28;47(16):4636–4643. doi: 10.1021/bi7019386

Figure 5.

Figure 5

Stereoview of the active sites of the dimer in crystal form 2 with 2Fo - Fc electron density, contoured at the 1.0σ level, for subunits A (top) and B (middle). Superposition of subunits A (in yellow) and B (in blue) is shown in the bottom panel. The β-mercaptoethanol molecule is connected to the side chain of Cys195 by a disulfide bond in subunit B while it forms a noncovalent adduct in subunit A. The distances from Cys195 to Ser216 are also different. Different oxidation states of Cys195 reflect its propensity to oxidation.