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![[Figure 5]](qe5005fig5mag.jpg)
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Figure 5
FutA (ferric state) determined by neutron diffraction at 2.1 Å resolution. The iron-binding site is formed by four tyrosines (Tyr13, Tyr143, Tyr199 and Tyr200), a solvent molecule (W1) and Arg103 in the second coordination shell. The positive density (green mesh, mFo − DFc omit map at the +3.0σ level) indicates that these atoms have undergone 1H/2H exchange and suggests that Arg103 is positively charged whilst W1 is neutral. The side chain of Arg203 is not oriented towards the binding site and does not engage in polar interactions. N, C and O atoms are shown in blue, dark green and red, respectively. Iron is shown in gold and H atoms are in grey. |
![[Figure 5]](qe5005fig5.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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