Fig. 2 BRD1389 binds at the active site of Plasmodium cFRS. a Structural organization of Pv cFRS α - and β -subunits. b Overall structure of Pv cFRS showing functional biological heterotetrametric assembly ( αβ ) 2 with two crystallographic heterodimers ( αβ ). The domain boundaries are labelled according to Tt FRS ( PDB “ 2IY5 [https://www.rcsb.org/structure/2IY5] ” ). The α -subunit consists of two domains: PA1 (catalytic domain, CAT) and PA2 domain. The β - subunit consists of PB1, PB3 (editing domain), PB4, PB5 and PB6-B7 (catalytic-like, CAM). c Surface view of Pv cFRS:BRD1389 complex depicting α -subunit (grey), β -subunit (pink) and bound BRD1389 (green) in the α -subunit. d The composite simulated annealed omit (SA-omit) (orange) and the fi nal 2F o -F c (blue) maps are contoured at 1 σ levels for the bound BRD1389. The fi nal 2F o -F c (blue) map clearly shows the continuous electron density for the bound