Fig. 2

Comparison of the di-copper centers from different type III copper proteins. (a) A. gambiae PPO8 (AgPPO8), PDB ID 4YZW; (b) M. sexta PPO1 (MsPPO1), 3HHS-B; (c) M. sexta PPO2 (MsPPO2), 3HHS-A; (d) Marsupenaeus japonicus (Mj) PPOβ, 3WKY; (e) Limulus polyphemus hemocyanin deoxy state (LpHc), 1LLA; (f) Octopus hemocyanin functional unit Odg, 1JS8; (g) Ipomoea batatas catechol oxidase (IbCO) in complex with 1-phenyl-2-thiourea (PTU), 1BUG; (h) Vitis vinifera catechol oxidase (VvCO), 2P3X; (i) Streptomyces castaneoglobisporus tyrosinase (ScTyr), 2ZMX; (j) Agaricus bisporus tyrosinase (AbTyr), 2Y9W; (k) Aspergillus oryzae pro-tyrosinase (AoProTyr), 3W6W; (l) Superposition of BmTyr structures in complex with bound tyrosine (4P6R) and L-DOPA (4P6S) (BmTyr:T/D); (m) Superposition of the active sites from AgPPO8, ScTyr, AoProTyr, LpHc and BmTyr:D. Space overlapping between the placeholders and phenolic substrate is indicated by a red dashed cycle. The Cu or Zn atoms are shown as large brown or gray spheres, the Cu-coordinated or hydrogen-bonded water molecules are shown as small red spheres. The hydrogen bonds are indicated as black dashes