Ligand Discovery for the Alanine-Serine-Cysteine Transporter (ASCT2, SLC1A5) from Homology Modeling and Virtual Screening
Fig 6
Outward-open conformation reveals an additional novel pocket.
(A) Predicted binding mode of the known inhibitor benzylcysteine derived from docking. The backbone atoms of ASCT2 are visualized as gray cartoon, with key residues establishing hydrogen bonds with the ligand in gray sticks, with oxygen, nitrogen, and hydrogen atoms in red, blue, and white, respectively. Two potential rotamers of Asp460 including the orientation facing the binding site (in pink) and surface (gray) are shown as sticks. Sodium ions are represented in purple spheres. (B) The binding site surface of the outward-open model of ASCT2 bound to benzylcysteine reveals the novel pocket (pocket A) resulting from the opening of HP2.