1N3P
Pterocarpus angolensis lectin in complex with sucrose
Summary for 1N3P
Entry DOI | 10.2210/pdb1n3p/pdb |
Related | 1N3O 1N3Q |
Related PRD ID | PRD_900003 |
Descriptor | lectin PAL, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total) |
Functional Keywords | lectin, carbohydrate recognition, sucrose, sugar binding protein |
Biological source | Pterocarpus angolensis |
Total number of polymer chains | 2 |
Total formula weight | 56025.28 |
Authors | Loris, R.,Imberty, A.,Beeckmans, S.,Van Driessche, E.,Read, J.S.,Bouckaert, J.,De Greve, H.,Buts, L.,Wyns, L. (deposition date: 2002-10-29, release date: 2002-11-20, Last modification date: 2024-03-13) |
Primary citation | Loris, R.,Imberty, A.,Beeckmans, S.,Van Driessche, E.,Read, J.S.,Bouckaert, J.,De Greve, H.,Buts, L.,Wyns, L. Crystal structure of Pterocarpus angolensis lectin in complex with glucose, sucrose, and turanose J.BIOL.CHEM., 278:16297-16303, 2003 Cited by PubMed Abstract: The crystal structure of the Man/Glc-specific seed lectin from Pterocarpus angolensis was determined in complex with methyl-alpha-d-glucose, sucrose, and turanose. The carbohydrate binding site contains a classic Man/Glc type specificity loop. Its metal binding loop on the other hand is of the long type, different from what is observed in other Man/Glc-specific legume lectins. Glucose binding in the primary binding site is reminiscent of the glucose complexes of concanavalin A and lentil lectin. Sucrose is found to be bound in a conformation similar as seen in the binding site of lentil lectin. A direct hydrogen bond between Ser-137(OG) to Fru(O2) in Pterocarpus angolensis lectin replaces a water-mediated interaction in the equivalent complex of lentil lectin. In the turanose complex, the binding site of the first molecule in the asymmetric unit contains the alphaGlc1-3betaFruf form of furanose while the second molecule contains the alphaGlc1-3betaFrup form in its binding site. PubMed: 12595543DOI: 10.1074/jbc.M211148200 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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