2.6.1.79	pyridoxal 5'-phosphate	required, stabilizes the enzyme	
2.6.1.79	pyridoxal 5'-phosphate	-	
2.6.1.79	pyridoxal 5'-phosphate	tightly bound to the enzyme	
2.6.1.79	pyridoxal 5'-phosphate	PLP, dependent on, PLP is bound in the active site of each chain in the wild-type structure. In the AtPAT crystal structure, PLP is covalently linked to the epsilon-nitrogen of Lys306 to form the internal aldimine (i.e. Schiff base). Trp193 and Ile274 position the ring of PLP through pi-pi stacking and van der Waals interactions, respectively. The pyridine ring nitrogen of PLP forms a charge-charge interaction with the side chain of Asp272