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Function of your protein

Biological relevance and broader implications

Important amino acids

Amino Acids in the are Lys 292, Asp 263, Arg 180. They are essential to the active site by providing certain . PLP is covalently bonded to the amino acid lysine. The nitrogen in the ring of PLP interacts with the negatively charged oxygen in the aspartate side chain. The phosphate group interacts with the positively charged nitrogen of the arginine side chain.

Structural highlights

The for PLP are semi-exposed to the "outside world" but also slightly hidden into the protein. Having binding pockets only slightly exposed can help prevent other competitive substrates from binding and and inhibiting the enzyme. The substrate PLP has a phosphate group that is surrounded by other polar amino acids but the rest of the substrate, the carbons are surrounded by other non-polar amino acids to satisfy the needs of the . PLP would not be very stable if the polar/hydrophilic portions of the substrate were trying to interact with all surrounding non-polar/hydrophobic amino acids. This allows interactions such as hydrogen bonding and pi-stacking to stabilize and bind a substrate in an active site.