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. Author manuscript; available in PMC: 2010 Jul 20.

Published in final edited form as: Dalton Trans. 2008 Jun 27;(38):5132–5142. doi: 10.1039/b803512a

Fig. 3 — Structure of XanA according to a homology model. (A) The predicted overall fold of the XanA protein is depicted as a green ribbon. (B) A blow-up of the proposed active site. In both panels, Fe^II is an orange sphere, αKG has yellow carbon atoms, metal ligands have blue carbon atoms, a cofactor-stabilizing residue (Arg 352) is shown with orange carbon atoms, and other postulated active site residues are indicated with white carbon atoms.

Fig. 3 — Structure of XanA according to a homology model. (A) The predicted overall fold of the XanA protein is depicted as a green ribbon. (B) A blow-up of the proposed active site. In both panels, Fe^II is an orange sphere, αKG has yellow carbon atoms, metal ligands have blue carbon atoms, a cofactor-stabilizing residue (Arg 352) is shown with orange carbon atoms, and other postulated active site residues are indicated with white carbon atoms.