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Figure 3
(a) Crystal structure of the FAW–DSM#1 complex. The molecular surface of the protein shows excellent shape complementarity between the ligands and the protein binding sites. DSM molecules I, II, III and IV (numbering as for FAF–DSM in Fig. 2[link]) are shown in space-filling representation. (b) The interactions stabilizing DSM molecules I and II in the β-barrel sites of subunit A: hydrogen bonds (red dashed lines), hydrophobic contacts or C—H⋯π interactions (black dotted lines) and ππ stacking interactions (blue dotted lines). (c) DSM IV in subunit B is additionally stabilized by a hydrogen bond to Glu158′ from a symmetry-related molecule (marked by a prime). (d) Shape complementarity between DSM III and the binding site at the dimer interface (green, subunit A; pink, subunit B). (e) Shape of the binding sites in the β-barrel interior (DSM I) and β-barrel entrance (DSM II) of subunit A. DSM II at the β-barrel entrance is additionally stabilized by the EF loop from a symmetry-related FAW molecule. (f)–(i) 2FoFc electron-density map contoured at 1.0σ around DSM ligand molecules I, II, III and IV (difference omit maps are presented in Supplementary Fig. S1).

Volume 9| Part 3| May 2022| Pages 386-398
ISSN: 2052-2525