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1N3P

Pterocarpus angolensis lectin in complex with sucrose

Summary for 1N3P
Entry DOI10.2210/pdb1n3p/pdb
Related1N3O 1N3Q
Related PRD IDPRD_900003
Descriptorlectin PAL, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, MANGANESE (II) ION, ... (5 entities in total)
Functional Keywordslectin, carbohydrate recognition, sucrose, sugar binding protein
Biological sourcePterocarpus angolensis
Total number of polymer chains2
Total formula weight56025.28
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 citationLoris, 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: 12595543
DOI: 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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