Fig. 4

Protein sequence alignment of 403 amino acid residues. Secondary structure prediction was based on structures of barley 1AMY (blue) and rice 3WN6 (red) with α-helices displayed as coils, β-strands as arrows, strict β-turns as TT letters, active sites as triangles, Ca²⁺ binding sites as stars and catalytic sites as circles. Domain A: a (β/α)₈-barrel of 286 residues, domain B: 64 residues, connecting strand β₃ and helix α₄ of the barrel, domain C: 53 residues forming a five stranded anti-parallel β-sheet. Two amino acids (Arg₉₇ and Asn₂₃₃), specific to Amy1λ proteins, were highlighted in pink