 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](no5180fig3mag.jpg)
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Figure 3
Multiple sequence alignment of FdR9 and homologous ferredoxin reductases obtained from a DALI search using the FdR9 structure as a template. Helices are represented by coils and β-sheets are shown as arrows. Columns with residues that are more than 70% similar according to physicochemical properties (threshold set to 0.7) are framed in blue and amino-acid residues with 100% identity are highlighted by a red background. FdR9 residues involved in hydrogen-bond interactions with the FAD molecule are framed in green boxes. The three loops of BphA4 interacting with the NAD molecule are framed in black boxes, and the residues of BphA4 interacting with the NAD molecule by hydrogen bonding and hydrophobic interactions are highlighted by yellow boxes. The PAM250 matrix was used for sequence alignment. The figure was rendered by ESPript 3.0 (Robert & Gouet, 2014  ). |
![[Figure 3]](no5180fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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