2-methylpropyl 2-oxo-4-phenylazetidine-1-carboxylate |
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site |
Escherichia coli |
|
cyclopentyl 2-oxo-4-phenylazetidine-1-carboxylate |
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site |
Escherichia coli |
|
phenyl 2-oxo-4-phenylazetidine-1-carboxylate |
beta-lactam inhibitor, forms a single bond to the catalytic serine and the carbonyl oxygen of the inhibitor faces away from the oxyanion hole. The hydrophobic N-substituent of the inhibitor points into a cavity within the enzyme, providing a structural explanation for the specificity of beta-lactams on rhomboid proteases. This same cavity probably represents the S2' substrate binding site |
Escherichia coli |
|