In this paper, we presented the 3D structure of multivalent compounds displaying chondroitin sulfate E (CS-E) disaccharide ligands and their interaction with langerin. The disaccharides correspond to the two alternative sequences of CS-E: GlcA-GalNAc and GalNAc-GlcA. Firstly, we studied the 3D structure of the two corresponding series of glycodendrimers free and in the presence of langerin. The structures of the free compounds are compatible with the expected ones. Both sequences exhibit very similar conformations with a rigid disaccharide, and a flexible region, the rest of the molecule. A key aspect of this work is the analysis of how different compounds interact with alternative regions of the langerin receptor as a function of the spatial distribution of the same binding epitope. This allows us to gain unique insights into the receptor's binding behaviour and the specific interactions mediated by different ligand valencies. We conducted NOESY experiments in the presence of langerin, concluding that the conformations of saccharides do not change upon binding. We performed STD-NMR experiments, showing that the monovalent compound with the GlcA at the non-reducing end can interact with langerin through the Ca2+ cation, while the reverse sequence does not. Trimers 2 and 6 interact mainly via the central aromatic core, independently of the disaccharidic sequence. In the case of the tetramer 3, the interaction takes place mainly by the GalNAc proton in position 4 and in the hexamer, a significant spin diffusion prevents the epitope analysis although the interaction with langerin was clearly observed. The STD-NMR experiments without Ca2+ showed a lack of binding for both monovalent compounds 1 and 5. In contrast, in the case of the multivalent compounds, 2, 3 and 6, STD peaks characteristics of binding were found with a similar pattern epitope maps to those obtained in the presence of Ca2+. We also performed DOSY experiments for the first series of GlcA-GalNAc compounds individually, in the presence and absence of langerin, and for the mixture of all the compounds in the same NMR tube. Finally, we performed MD simulations for the monovalent and trivalent compounds, supporting the NMR conclusions.