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![[Figure 3]](ag5030fig3mag.jpg)
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Figure 3
Liganded structures of Hmo. (a) Superposition of ternary complexes of wild-type Hmo on those of the Y128F mutant shows a low average root-mean-square deviation (r.m.s.d.) of 0.064 Å, where Hmo and the Y128F mutant are colored cyan and green, respectively. There is no significant difference between Hmo (green) and the Y128F mutant (cyan) in terms of the active-site geometry, except that the p-OH group is absent on the phenyl ring of Y128F. (b) When Hmo is bound by (S)-mandelate, Met160 flips away and Arg163 makes an electrostatic association with the carboxylic group of (S)-mandelate. (c) When benzoylformate is bound to Hmo, it adopts double conformations (pro-S or pro-R). Met160 stows back, while Arg163 flips away. The numbers are bond lengths in Å for the designated bonds. Free ligands, FMN and active-site residues are colored cyan, yellow and green, respectively. The 2Fo − Fc electron-density map is contoured at 2σ. |
![[Figure 3]](ag5030fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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