Serine Protease Active Sites

Three Serine Proteases - Chymotrypsin, Elastase and Trypsin - with Covalently Modified Active Sites	Inhibitory Molecules
	P-Sulfinotoluene TOS		M-Amidinophenyl-3-Alanine (2S)-2-amino-3-(3-carbamimidoylphenyl)propanoic acid
Active Site I	Active Site II		Active Site III

Atom colors are colored according to modified CPK colors where non-basic N atoms are colored lavender; basic N atoms are colored a blue; non-acidic O atoms are colored pink; and acidic O atoms are colored a brighter red.		The carbon atoms of the amino acid residues forming the "catalytic triad" in each enzyme active site are colored in dark gray. The carbon atoms of Asp₁₉₄ outside the enzyme active site are colored in light turquoise. The carbon atoms of the TOS and/or the amidinophenyl-3-alanine inhibitors are colored dark green.