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. 2021 Sep 27;77(Pt 10):1251–1269. doi: 10.1107/S2059798321009025

Figure 9.

Figure 9

The active site and protonation states of glutamate residues with backbone carbonyl O atoms (PDB entry 6kk8, H/D exchanged; Yamada et al., 2019). 2F oF c NSLD map (σ = 1.00) is displayed as a blue mesh; H and D atoms are displayed in white and turquoise, respectively. (a) Manganese catalase active site with the bridging O atoms coordinated to the two manganese cofactors. Bridging atoms O1004 and O1005 have alternate conformations, which are shown in red and pale red. (b) Single protonation of Glu167 forming a hydrogen bond to the Ala279 carbonyl group oxygen. (c) Single protonation of Glu280 forming a hydrogen bond to the Phe116 carbonyl group oxygen.