Structure of glycogen phosphorylase. This enzyme forms a homodimer: one subunit is shown in white and the other in yellow. Each catalytic site includes a pyridoxal phosphate (PLP) group, linked to lysine 680 of the enzyme. The binding site for the phosphate (Pi) substrate is shown. Notice that the catalytic site lies between the C-terminal domain and the glycogen-binding site. A narrow crevice, which binds four or five glucose units of glycogen, connects the two sites. The separation of the sites allows the catalytic site to phosphorolyze several glucose units before the enzyme must rebind the glycogen substrate.
[Drawn from 1NOI.pdb.]