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![[Figure 4]](fs5171fig4mag.jpg)
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Figure 4
Active site of NcLPMO9D in the enzymatic resting state (PDB entry 5tki; O'Dell et al., 2017  ). The conformation and tautomeric state of the singly protonated His157 revealed by neutron protein crystallography was confirmed to stabilize molecular oxygen (not shown) near the active site of LPMO by quantum-chemical calculations. The H1 backbone amide N and carbonyl O atoms form hydrogen bonds to the `pocket' water molecule, which has been hypothesized to participate in substrate interactions. 1H atoms are shown in light gray, while atoms that have undergone exchange to 2H are shown in white. The Cu atom is shown in brown. The blue mesh represents a neutron SLD 2Fo − Fc map contoured at σ = 1.0. Reproduced from Schröder et al. (2018). |
![[Figure 4]](fs5171fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
