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![[Figure 3]](fs5171fig3mag.jpg)
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Figure 3
HIV-1 protease in complex with the clinical drug darunavir (PDB entries 5e5j and 5e5k; Gerlits et al., 2016  ). Upon homodimerization, the catalytic site contains two closely positioned aspartic acid residues. (a) At pH 4.3, darunavir accepts a hydrogen bond from Ala25 and donates a hydrogen bond to Ala25′. (b) At pH 6.0, the two hydrogens undergo a transfer reaction in the catalytic site, which was captured for the first time by neutron crystallography. C atoms belonging to darunavir are colored green. 1H atoms are shown in light gray, while atoms that have undergone exchange to 2H are shown in white. The blue mesh represents neutron SLD 2Fo − Fc maps contoured at σ = 1.0. Reproduced from Schröder et al. (2018). |
![[Figure 3]](fs5171fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
