Extended Data Fig. 3: Additional ligand-bound crystal structure complexes.
From: Mechanistic plasticity in ApmA enables aminoglycoside promiscuity for resistance
(a) Amino acids implicated in positioning kanamycin B. All of the observed AG ligands, (b) tobramycin and (c) kanamycin B, bound to ApmA are superimposed. Each ring is identified with a roman numeral and site of acetylation is labelled. (d) Amino acids implicated in positioning gentamicin C1a. (e) Each gentamicin bound to ApmA is superimposed for analysis of sugar ring conformations within each binding pocket. Panel e also highlights torsional angle differences for glycosidic linkages ΦII/III and ψII/III.
