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Table 4 Residues involved with HETA binding to the three MTAPs

From: Leishmania infantum 5’-Methylthioadenosine Phosphorylase presents relevant structural divergence to constitute a potential drug target

huMTAP T18 H65 P69 A94 C95 G96 F177 I194 N195 M196 T197 T219 D220 D222 V231 V236
Li MTAP G16 G17 R60 H61 H65 N68 P69 I92 N93 A94 F181 G199 M200 T201 M221 M243
Tb MTAP G18 H62 H66 V93 N94 A95 V96 F185 M204 A225 T227 M247 N250 V251 V254
MEME motifs 5 5 2 2 2 2 2 3 3 3 3 3 1 1 1 1 1 1 1 1 1 1 4 4 4 4
  1. The table illustrates interacting residues with HETA at a distance lower than or equal to a cutoff of 4Ǻ. Residues listed in the same column are structurally aligned IRs. Residues were observed that interact in the three MTAPs with both MTA and HETA. Residues specifically involved with HETA binding (vs. MTA) are shown in bold