Trypsin is a globular serine protease enzyme featuring a well-defined tertiary structure composed primarily of two distinct beta-barrel domains connected by surface loops and stabilized by conserved disulfide bonds. Its overall architecture creates a deep catalytic cleft where the active site residues—specifically a catalytic triad consisting of histidine, aspartate, and serine—are precisely positioned to cleave peptide bonds on the carboxyl side of lysine and arginine residues. The structural rigidity and precise spatial orientation of its substrate-binding pocket ensure high enzymatic specificity, allowing trypsin to function efficiently in protein digestion and biochemical processing.