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![[Figure 3]](di5009fig3mag.jpg)
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Figure 3
Cadmium ion-binding sites in HEWL and ETR1. (a) Cadmium ions binding at the active site of HEWL. A novel cadmium-chloride cluster is present in the active site and bridges the active-site residues Glu35 and Asp52. Active-site residues and ethanediol (EDO) are shown as sticks. Cadmium ions (cyan), chloride ions (green) and water molecules (red) are shown as spheres. The anomalous difference map contoured at 6σ is shown in purple. (b) Formation of crystal contacts by cadmium ions in ETR1. A cadmium ion (Cd605) and its symmetry equivalent bridge residues His420 and Glu451. Protein residues are shown as sticks. Parts of the protein chains are shown as cartoons in grey and orange (symmetry-related molecule). Cadmium ions (cyan) and water molecules (red) are shown as spheres. Symmetry-related residues are highlighted with an asterisk. The anomalous difference map contoured at 18σ is shown in purple. |
![[Figure 3]](di5009fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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