6RZI
Galectin-3C in complex with trifluoroaryltriazole monothiogalactoside derivative:1(Hydrogen)
Summary for 6RZI
| Entry DOI | 10.2210/pdb6rzi/pdb |
| Descriptor | Galectin-3, (2~{R},3~{R},4~{S},5~{R},6~{R})-2-(hydroxymethyl)-6-phenylsulfanyl-4-[4-[3,4,5-tris(fluoranyl)phenyl]-1,2,3-triazol-1-yl]oxane-3,5-diol, THIOCYANATE ION, ... (4 entities in total) |
| Functional Keywords | lectin, carbohydrate-binding protein, galactose-specific lectin 3, galactoside-binding protein, galbp, ige-6 binding protein, l-31, laminin-binding protein, lectin l-29, mac-2, sugar binding protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 16212.57 |
| Authors | Kumar, R.,Verteramo, M.L.,Nilsson, U.J.,Logan, D.T. (deposition date: 2019-06-13, release date: 2020-07-08, Last modification date: 2025-01-08) |
| Primary citation | Verteramo, M.L.,Ignjatovic, M.M.,Kumar, R.,Wernersson, S.,Ekberg, V.,Wallerstein, J.,Carlstrom, G.,Chadimova, V.,Leffler, H.,Zetterberg, F.,Logan, D.T.,Ryde, U.,Akke, M.,Nilsson, U.J. Interplay of halogen bonding and solvation in protein-ligand binding. Iscience, 27:109636-109636, 2024 Cited by PubMed Abstract: Halogen bonding is increasingly utilized in efforts to achieve high affinity and selectivity of molecules designed to bind proteins, making it paramount to understand the relationship between structure, dynamics, and thermodynamic driving forces. We present a detailed analysis addressing this problem using a series of protein-ligand complexes involving single halogen substitutions - F, Cl, Br, and I - and nearly identical structures. Isothermal titration calorimetry reveals an increasingly favorable binding enthalpy from F to I that correlates with the halogen size and σ-hole electropositive character, but is partially counteracted by unfavorable entropy, which is constant from F to Cl and Br, but worse for I. Consequently, the binding free energy is roughly equal for Cl, Br, and I. QM and solvation-free-energy calculations reflect an intricate balance between halogen bonding, hydrogen bonds, and solvation. These advances have the potential to aid future drug design initiatives involving halogenated compounds. PubMed: 38633000DOI: 10.1016/j.isci.2024.109636 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.095 Å) |
Structure validation
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