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![[Figure 5]](lv5066fig5mag.jpg)
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Figure 5
Structures of the T2/T3 copper sites in (a) BaL and (b) MaL. The amino-acid residues are shown as ball-and-stick models and are coloured according to atom type. The C atoms of the His residues coordinated to the Cu31, Cu32 and Cu2 ions are shown in dark green, light green and gold, respectively. The oxygen ligands and the chloride ion are displayed as ball-and-stick models in red and grey, respectively. The copper ions are represented as orange spheres. The 2Fo − Fc electron-density map (at the 1.0σ level) is shown in magenta. Coordination bonds are indicated by black dashed lines. The weak coordination bond between Cu31 and His429 Nδ is shown as a violet dashed line. The structure of MaL from PDB entry 2q9o was used (Hakulinen et al., 2002  ). |
![[Figure 5]](lv5066fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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