 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](cb5072fig1mag.jpg)
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Figure 1
(a) Structure of CmArsM with bound PhAs(III). Cartoon diagram (colored in light orange) representation of PhAs(III)-bound CmArsM (PDB entry 4kw7 ). The conserved cysteine residues are shown in ball-and-stick representation and are colored green (carbon), blue (nitrogen) or yellow (sulfur). The dark blue sphere is the As atom and the light blue sphere is a Ca2+ ion in the SAM binding site. PhAs(III) is bound between the conserved residues Cys174 and Cys224. (b) A disulfide bond between Cys44 and Cys72. The four conserved cysteine residues are shown in ball-and-stick representation. The length of the disulfide bond is approximately 2.1 Å in the PhAs(III)-bound structure. |
![[Figure 1]](cb5072fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
