5WEY
Joint X-ray/neutron structure of Concanavalin A with alpha1-2 D-mannobiose
Summary for 5WEY
Entry DOI | 10.2210/pdb5wey/pdb |
Related PRD ID | PRD_900111 |
Descriptor | Concanavalin-A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total) |
Functional Keywords | lectin, carbohydrate complex, protonation state, hydrogen bonding, neutron crystallography, sugar binding protein |
Biological source | Canavalia ensiformis (Jack bean) More |
Total number of polymer chains | 1 |
Total formula weight | 26059.70 |
Authors | Kovalevsky, A.,Gerlits, O.O.,Woods, R.J. (deposition date: 2017-07-11, release date: 2017-09-13, Last modification date: 2023-10-04) |
Primary citation | Gerlits, O.O.,Coates, L.,Woods, R.J.,Kovalevsky, A. Mannobiose Binding Induces Changes in Hydrogen Bonding and Protonation States of Acidic Residues in Concanavalin A As Revealed by Neutron Crystallography. Biochemistry, 56:4747-4750, 2017 Cited by PubMed Abstract: Plant lectins are carbohydrate-binding proteins with various biomedical applications. Concanavalin A (Con A) holds promise in treating cancerous tumors. To better understand the Con A carbohydrate binding specificity, we obtained a room-temperature neutron structure of this legume lectin in complex with a disaccharide Manα1-2Man, mannobiose. The neutron structure afforded direct visualization of the hydrogen bonding between the protein and ligand, showing that the ligand is able to alter both protonation states and interactions for residues located close to and distant from the binding site. An unprecedented low-barrier hydrogen bond was observed forming between the carboxylic side chains of Asp28 and Glu8, with the D atom positioned equidistant from the oxygen atoms having an O···D···O angle of 101.5°. PubMed: 28846383DOI: 10.1021/acs.biochem.7b00654 PDB entries with the same primary citation |
Experimental method | NEUTRON DIFFRACTION (2.5 Å) X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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