view article
Figure 5
(a) Comparison of the active-site residues of Rv1625c-F363R (blue) with active (PDB entry 1cjk ; yellow) and inactive (PDB entry 1ab8 ; pink) forms of mAC. The active-site residues of Rv1625c-F363R are shown in grey and labelled. The substrate analogue ATPαS-Rp and metal ions bound in the active mAC structure are shown in stick and sphere representations, respectively. (b) Salt bridges formed by the catalytic aspartate Asp296 with Arg344 are shown.

IUCrJ
Volume 1| Part 5| August 2014| Pages 338-348
ISSN: 2052-2525
doi:10.1107/S2052252514016741