Structure of a leukotriene A4 hydrolase in complex with bestatin. The overall fold of this metalloprotease is similar to that of bacterial thermolysin. The catalytic domain consists of two subdomains. The N-terminal subdomain contains three beta sheets, whereas the C-terminal subdomain is mainly helical. The catalytic site of this protease contains a Zn atom (shown as a golden sphere) complexed by His296, His300, and Glu319. It also contains Glu297, which is supposed to provide a general base to attack the target peptidic bond by interacting with a water molecule, and Tyr384, which is the putative general acid that helps the release of the product.
Structures are rendered as ribbons. Catalytic and catalytic metal-complexing residues are shown as neons. Inhibitors are displayed as space filling spheres.
Carbons are shown in light gray, hydrogens in cyan, oxygens in red, nitrogens in blue, and sulfurs in yellow.
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