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![[Figure 6]](nz5013fig6mag.jpg)
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Figure 6
5-Nitrosalicylate (tan) and 5-chlorosalicylate (light green) docked into the active site of 5NSDO (a) and the experimentally observed bidentate binding mode of gentisate in SDO (b) (PDB entry 3nl1). The histidine residues involved in the coordination of iron(II) are colored cyan. The residues which have been experimentally shown to be involved in substrate coordination and/or discrimination, and that are important for the catalytic activity of SDO, are depicted in purple in (b), with the homologous residues in 5NSDO highlighted in the same color in (a). Met46 and Leu38 in the N-terminal part of the neighboring subunit in the SDO–gentisate complex (see text) are omitted for clarity. |
![[Figure 6]](nz5013fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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