Fig. 3: Detailed view of MsmCoaBC active sites and MsmCoaB dimerisation interface.
From: Inhibiting Mycobacterium tuberculosis CoaBC by targeting an allosteric site
a View of CoaC active site with FMN bound. The active site sits between two protomers of one trimer (gold and pink) and a third protomer from an adjacent trimer (green). Hydrogen bonds are depicted in yellow and π-interactions are in blue. b Superposition of a CoaB crystal structure in green, with full-length CoaBC (teal) showing the active site flaps (brown) of the CoaB and CoaC enzymes. c Detailed view of the CTP binding site. Cartoon and residues belonging to each protomer are coloured differently. Hydrogen bonds and π-interactions are coloured as in b. Important waters are represented as red spheres and calcium as a green sphere. Calcium coordination is depicted in purple. d CoaB dimerisation interface. Each protomer is coloured as in c.
