Savinase protease enzyme

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Savinase, a serine protease, is commonly observed due to its widespread usage as an enzyme in detergents. This remarkable enzyme breaks down proteins into smaller fragments by hydrolyzing the peptide bonds that hold amino acids together. Savinase accomplishes this through a catalytic triad, where three amino acids work together to launch a powerful nucleophilic assault on peptide bonds. In savinase, aspartate 32 forms a hydrogen bond with histidine 64, increasing the pKa of the imidazole ring and enabling it to deprotonate serine 221, which then attacks and breaks the peptide bond of a bound substrate. Despite the aspartate, histidine, and serine residues being distant in savinase's backbone, their specific three-dimensional folding brings them close enough to perform their catalytic function. Substrates bind in the ridge easily found on the enzyme's printed structure. Only the histidine and serine residues are visible in surface renders; the aspartate lies deeper within the enzyme, behind the histidine (indicated by purple dots). For optimal results, set layer height at .1, infill at .2 to .4, and use sufficient infill to prevent wasting filament on a bulky molecule. Due to the complex structure of proteins, supports are necessary, but removing them can be time-consuming, making it an exploration of the protein's intricate design.