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Figure 5
The structure of the complex of PigF with the cofactor SAH. (a) The structure of the PigF dimer present in the asymmetric unit with the cofactor SAH. The dimerization domain of subunit A is coloured blue and the catalytic domain is coloured violet. Subunit B is coloured grey. SAH and acetate (ACT) are shown as orange and yellow sticks, respectively. (b) Chain A of PigF with the cofactor SAH. Individual domains are coloured blue and violet, respectively. SAH (C atoms in orange) is shown in the SAH binding domain. (c) The SAH binding site. SAH is coloured orange, residues are shown as magenta sticks, water molecules are shown as yellow spheres and hydrogen bonds are shown as dotted lines and coloured black; the cartoon representation of the PigF–SAH structure is shown with 80% transparency.

IUCrJ
Volume 9| Part 2| March 2022| Pages 316-327
ISSN: 2052-2525
https://doi.org/10.1107/S2052252521011696