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![[Figure 2]](jc5060fig2mag.jpg)
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Figure 2
Crystal structure of DmmarA. (a) Overall structure of DmmarA. The front view is shown on the left, the side view in the middle and the bottom view on the right. Chain A is displayed as a blue cartoon and chain B as a light blue cartoon. Amino acids forming the catalytic pentad are visualized as green spheres. The L5 loop is coloured purple. (b) Stereo 2Fo − Fc electron-density map contoured at 2σ for key active-site residues (grey mesh). Protein residues are shown as blue sticks and water as a red sphere. (c) Active sites of DmmarA and HanR. The left panel depicts the active site of DmmarA. Residues in the proton-relay system, halide-binding site and access tunnel are displayed as blue sticks. Unique residues are highlighted as semi-transparent spheres. Hydrogen bonds between residues and to water are shown as yellow dashed lines. Water is visualized as a red sphere. The middle panel displays a superposition of the active sites of DmmarA (blue) and HanR (gold). The right panel shows the active site of HanR. The residues are displayed as gold sticks; hydrogen bonds between residues and the coordination of a chloride ion are shown as yellow dashed lines. The chloride ion is visualized as a green sphere. |
![[Figure 2]](jc5060fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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