Figure 3
(a) Crystal packing in the dimeric crystal structure of a glutathione-dependent lyase LigG solved at 1.1 Å resolution (PDB code 4yap) (Pereira et al., 2016), showing the SO42− anion bound to the surface region participating in the crystal lattice. (b) Zoom in showing the LigG crystal contact with the hydrogen bonds and salt bridges observed between SO42− and the symmetry-related copies of LigG. The SO42− contacts Arg43 via the main chain N atom and NE and NH2 from the side chain. The positive residue Arg43 makes a salt bridge interaction with the symmetry-related residue Glu208. The SO42− ion makes additional contacts with the main chain N atoms of Glu208 and Lys207. The NZ atom of Lys207 makes a hydrogen bond with the carbonyl group of Arg43. A 2mFo–DFc electron density map contoured at 1.5σ is shown in blue. Contacts are shown as broken lines and distances in ångströms. |