Naegleria fowleri: Protein structures to facilitate drug discovery for the deadly, pathogenic free-living amoeba
Fig 3
A. Quaternary structure of NfPRMT1 (6CU5) with chain A and B colored blue and green respectively with SAH ligands in red. B. Structural alignment of Chain A HsPRMT1 (6NT2) and Chain A NfPRMT1 (6CU5) colored pink and blue respectively with SAH ligand and GSK3368715 colored yellow and red respectively. C. Depiction of the electron density surrounding the GSK3368715 inhibitor from the 6NT2 model. |Fo|–|Fc| electron density omit map shown sculpted around GSK3368715 inhibitor at 2.0 Å, calculated using the composite-omit-map function of Phenix [25]. N-terminal residues which contact the ligand within 4 Å are shown in ball and stick (blue:nitrogen; red: oxygen; gray:carbon) and are labelled. All labelled residues are within the allosteric inhibition site of HsPRMT1.