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. Author manuscript; available in PMC: 2007 Dec 1.

Published in final edited form as: Bioorg Chem. 2006 Oct 27;34(6):394–409. doi: 10.1016/j.bioorg.2006.09.007

The active site of NaBH₄ reduced phosphonatase. (A) Depicted with the electron density surrounding the modified Lys53. The active site residues (yellow) and ligands sulphate (orange) and cofactor Mg²⁺ (cyan) are depicted as ball-and -stick. The 2Fo-Fc electron density map (contoured at 1.5 σ) is shown as blue cages. (B). Chemdraw depiction of Ne-ethy-Lys53 and surrounding active-site residues (distances in Å).

The active site of NaBH₄ reduced phosphonatase. (A) Depicted with the electron density surrounding the modified Lys53. The active site residues (yellow) and ligands sulphate (orange) and cofactor Mg²⁺ (cyan) are depicted as ball-and -stick. The 2Fo-Fc electron density map (contoured at 1.5 σ) is shown as blue cages. (B). Chemdraw depiction of Ne-ethy-Lys53 and surrounding active-site residues (distances in Å).