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![[Figure 4]](ji5017fig4mag.jpg)
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Figure 4
Environment surrounding the redox centres in CARDO-RJ3. (a) The network of hydrogen bonds around the [2Fe–2S] cluster. The individual domains and the [2Fe–2S] cluster are represented and coloured as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) . The [2Fe–2S] cluster is coordinated by cysteine residues 35, 40, 43 and 76 (labelled in bold). The side chains of Tyr33 and Leu74 create a hydrophobic environment within the cluster. Hydrogen bonds between the cluster sulfides and the surrounding residues are shown as orange dashed lines. (b) Relationships between redox centres. The difference density maps (Fo − Fc) of the [2Fe–2S] cluster and FAD in CARDO-RJ3 are displayed. Both cofactors were omitted for the calculation of the difference density maps, which are shown in blue and grey and contoured at 5.0σ and 2.5σ, respectively. Cys35 O provides the closest approach to C8M of FAD, with an average distance of 3.3 Å. Phe135 in the FAD-binding domain and Phe328 in the NADH-binding domain provide π-stacking interactions and Ala149 supports hydrophobic interaction with the FAD isoalloxazine ring. Arg148 in the FAD-binding domain and Trp56 in the Fd domain interact with adenine and the FAD-binding region via cation–π and π-stacking interactions, respectively. Phe329, which interacts with the Fd domain, is the C-terminal residue of the enzyme. (c) Hydrogen bonds between the FAD isoalloxazine ring and the surrounding residues (Ser151, Tyr165, Lys167 and Ser217) are shown. |
![[Figure 4]](ji5017fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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