Structure of homodimeric human renal dipeptidase complexed with cilastatin. Both monomers are bound by a disulfide bridge with Cys377.
The catalytic site of this protease contains two Zn atoms (shown as a golden spheres). Zinc 1 is complexed by His36 and Asp38, whereas zinc 2 is complexed by His214 and His235. On the other hand, Glu141 forms a "bridge" and complexes both atoms. According to its position, the putative general base which attacks the target peptidic bond depends on Asp304.



  • 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.

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