Fig. 2

Multiple sequence alignment and structural domain analysis of laccase proteins in P. eryngii and P. ostreatus. The signature sequences (a) and predicted substrate binding loops (b) in P. eryngii PeLac1-10 in comparison with those in P. ostreatus PoLac1-12. The histidine (H) and cysteine (C) residues are numbered according to the type of copper to which they bind (1, 2, and 3). Solid triangles below the sequences denote residues in the B4–B5 β-hairpin loop that are a highly conserved cysteine (C) and either an aspartic acid (D) or a glutamic acid (E) in classical laccases