Fig. 4: Catalytic sites in LH3.

a Enzymatic pocket in the GlcT domain. The UDP bound in the pocket was shown as stick model colored by elements. The Mn²⁺ ion was shown as a purple sphere. The interacting residues were shown as stick model colored by elements. b The enzymatic pocket in the LH domain. The 2-OG bound in the pocket was shown as stick model colored by elements. The Fe ion was shown as a brown sphere. The interacting residues were shown as stick model colored by elements. The non-proteinous density in the cryo-EM map near the catalytic site was shown and highlighted in yellow. c The galactosyltransferase and glucosyltransferase activities of the purified KOGG complex with mutations at the catalytic sites of GlcT and LH domain of LH3 (n = 3 biologically independent samples). Data are presented as mean values +/− SD. Source data are provided as a Source Data file. Data analysis was performed using one-way ANOVA with Dunnett’s multiple comparisons test. *, P-value < 0.05; **, P-value < 0.01; ***, P-value < 0.001; ****, P-value < 0.0001. d The lysyl hydroxylase activities of the purified KOGG complex with mutations at the catalytic site in the LH domain of LH3 (n = 3 biologically independent samples). Data are presented as mean values +/− SD. Source data are provided as a Source Data file. Data analysis was performed using one-way ANOVA with Dunnett’s multiple comparisons test. ***, P-value < 0.001; ****, P-value < 0.0001.