S-Adenosyl-S-carboxymethyl-l-homocysteine: a novel cofactor found in the putative tRNA-modifying enzyme CmoA

Byrne, R.T.; Whelan, F.; Aller, P.; Bird, L.E.; Dowle, A.; Lobley, C.M.C.; Reddivari, Y.; Nettleship, J.E.; Owens, R.J.; Antson, A.A.; Waterman, D.G.

doi:10.1107/S0907444913004939

Acta Crystallographica Section D
Acta Crystallographica
Section D STRUCTURAL BIOLOGY

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Figure 3
Structure of S-adenosyl-S-carboxymethyl-L-homocysteine (SCM-SAH). The final coordinates are displayed with (a) the likelihood-weighted mF_o − DF_c difference electron-density maps contoured at 3σ calculated prior to the modelling of SCM-SAH and (b) the 2mF_o − DF_c electron-density maps contoured at 1.5σ. The SCM-SAH model is shown with C atoms in cyan, O atoms in red and N atoms in blue. C atoms of protein residues are shown in green.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

Volume 69| Part 6| June 2013| Pages 1090-1098

https://doi.org/10.1107/S0907444913004939

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