Structure of human gamma-glutamyl hydrolase. The overall fold of this enzyme resembles that of class I glutamine amidotransferases. This similarity extends to the catalytic site, which features a charge relay system from Glu246 to His244 to Cys134. Interestingly, this fold does not resemble the fold of any other cysteine protease, which suggests that C26 peptidases evolved independently, perhaps from non-proteolytic enzymes. The charge relay system increases the nucleophilicity of the sulfur in the catalytic cysteine. Thus, the glutamate side chain interacts with the gamma hydrogen of the histidine. In other cysteine proteases, the role of the glutamate may be played by an asparte, an asparagine, a glutamine, a serine or a threonine. This interaction aligns the epsilon nitrogen of the histidine so that it forms a hydrogen bond with the beta hydrogen from the cysteine. You can click the render window and press '4' to see these interactions as translucid bars.
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.
Left-click and drag to rotate the protease. Right-click and drag up/down to zoom in/out. Click with both buttons and drag to move the protease. Use the upper bar to get different views and for display options. For a close-up of the catalytic site, choose the cat_site view.
Once you have clicked inside the structure window, you can use the keyboard to hide/show objects:
'1' toggles the ribbon. '2' toggles the inhibitor. '3' toggles the catalytic residues.