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5WEY

Joint X-ray/neutron structure of Concanavalin A with alpha1-2 D-mannobiose

Summary for 5WEY
Entry DOI10.2210/pdb5wey/pdb
Related PRD IDPRD_900111
DescriptorConcanavalin-A, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordslectin, carbohydrate complex, protonation state, hydrogen bonding, neutron crystallography, sugar binding protein
Biological sourceCanavalia ensiformis (Jack bean)
More
Total number of polymer chains1
Total formula weight26059.70
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 citationGerlits, 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: 28846383
DOI: 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

226707

건을2024-10-30부터공개중

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