1WBF
WINGED BEAN LECTIN, SACCHARIDE FREE FORM
Summary for 1WBF
Entry DOI | 10.2210/pdb1wbf/pdb |
Descriptor | PROTEIN (AGGLUTININ), 2-acetamido-2-deoxy-beta-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total) |
Functional Keywords | lectin (agglutinin), legume lectin, protein crystallography, blood group specificity, saccharide free form, sugar binding protein |
Biological source | Psophocarpus tetragonolobus (winged bean) |
Total number of polymer chains | 2 |
Total formula weight | 54348.46 |
Authors | Manoj, N.,Srinivas, V.R.,Suguna, K. (deposition date: 1998-12-16, release date: 1999-12-22, Last modification date: 2024-12-25) |
Primary citation | Manoj, N.,Srinivas, V.R.,Suguna, K. Structure of basic winged-bean lectin and a comparison with its saccharide-bound form. Acta Crystallogr.,Sect.D, 55:794-800, 1999 Cited by PubMed Abstract: The crystal structure of the saccharide-free form of the basic form of winged-bean agglutinin (WBAI) has been solved by the molecular-replacement method and refined at 2.3 A resolution. The final R factor is 19.7% for all data in the resolution range 8.0-2.3 A. The asymmetric unit contains two half-dimers, each located on a crystallographic twofold axis. The structure of the saccharide-free form is compared with that of the complex of WBAI with methyl-alpha-D-galactoside. The complex is composed of two dimers in the asymmetric unit. The intersubunit interactions in the dimer are nearly identical in the two structures. The binding site of the saccharide-free structure contains three ordered water molecules at positions similar to those of the hydroxyl groups of the carbohydrate which are hydrogen bonded to the protein. Superposition of the saccharide-binding sites of the two structures shows that the major changes involve expulsion of these ordered water molecules and a shift of about 0.6 A of the main-chain atoms of the variable loop. PubMed: 10089310DOI: 10.1107/S090744499900044X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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