The presence of key residues such as Glu 35, Asp 52 and Trp 62 in the binding pocket of the LYZ active center, which are related to the activity of LYZ, indicates that PHE preferentially binds to the active center of LYZ.
Key residues such as Glu 35, ASP 52 and Trp 62 related to Lyz activity exist in Lyz active center binding pocket, indicating that Phe preferentially binds to Lyz active center.<br>
The existence of key residues such as Glu 35, Asp 52 and Trp 62 related to LYZ activity in the binding pocket of LYZ active center indicates that PHE preferentially binds to LYZ active center.