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Crystallographic data of OAOR in complex with its two substrates reveals the str

ID: 67927 • Letter: C

Question

Crystallographic data of OAOR in complex with its two substrates reveals the structure of the enzyme's active site and Michaelis complex, shown below (the solid line indicates the surface of the protein). a. While the active site and oxaloacetate are both highly charged molecules, the crystallographic data indicates that a number of intermolecular forces, in addition to ionic contacts, are present in the the Michaelis complex. Clearly indicate these interactions in the figure below; note that some of these interactions do not occur with substrate and that a salt bridge does not preclude another type of interaction, such as an H-bond.

Explanation / Answer

There can be Vander Waal or hydrophobic interactions between the atoms.

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