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X-ray crystallography revealed that each monomer consists of: An 8-bladed -propeller domain (residues 61-495, colored green), which contains two substrate anchoring residues, Glu205, Glu206 (colored cyan) An / hydrolase domain (residues 39-55 and 497-766, colored magenta), which contains three catalytic residues, Ser630, His740, Asp708 (colored orange) The domain organization of the DPP-4 dimer is shown in Figure-2 and a view of the enzyme active site is shown in the inset

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