view article

Figure 4
Close-up view of the cofactor-binding sites. (a) Residues interacting with the cofactor. The corresponding 2FoFc electron-density maps of the cofactor and Lys274 are shown and contoured at 1.0σ. The cofactor in subunit A is PMP. The cofactor in subunit B is a mixture of PMP and PLP. Lys274 has multiple conformations in each monomer. (b) Interactions between Lys274 and the cofactor, Trp68 and Tyr306*. Hydrogen bonds are depicted as black dotted lines. Distances between the N atom of Lys274 and the C-4′ atom of the cofactor are depicted as red dotted lines. Distances in Å are displayed in red. The asterisk indicates the residue from the neighbouring subunit.

ISSN: 2053-230X
Volume 72| Part 6| June 2016| Pages 448-456
Follow Acta Cryst. F
Sign up for e-alerts
Follow Acta Cryst. on Twitter
Follow us on facebook
Sign up for RSS feeds