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Figure 2
Comparison of BeSAHase active sites: (a) the Ado-complexed subunit A from the Ado/Cord complex, (b) the Cord-complexed subunit D from the Ado/Cord complex, (c) the Ade-complexed subunit A from the Ade complex and (d) the 2′-dAdo-complexed subunit C from the Ade/2′-dAdo complex. Since the mode of binding of all Ado molecules in all respective complexes is identical, only the ligand from the Ado/Cord structure is shown. Similarly, as the mode of binding of all Ade ligands is identical, only Ade from the Ade complex is shown. The ligands and water molecules are shown in FoFc OMIT electron-density (calculated without the contribution of the nucleosides, Ade and water atoms to Fc). The maps are contoured at 4σ, 3σ, 3σ and 4σ, respectively.

Volume 4| Part 3| May 2017| Pages 271-282
ISSN: 2052-2525