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. 2009 Oct 6;106(40):17002–17006. doi: 10.1073/pnas.0906095106

Fig. 1.

Fig. 1.

Overall structure of M. sexta PPO. (A) The heterodimeric PPO is formed in a back-to-back mode. PPO1 and PPO2 are shown in green and yellow, respectively. (B) Domains of PPO2 are colored as follows: pro-region, purple; domain I, blue; domain II, yellow; domain III, green. The di-copper atoms are located in domain II and are shown as red spheres. The proteolytic site R51 residue is shown in the stick. The amino-terminus and carboxyl-terminus of PPO2 are indicated as N and C, respectively.