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2D7F

Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid

Summary for 2D7F
Entry DOI10.2210/pdb2d7f/pdb
Related1WUV
DescriptorConcanavalin A, methyl alpha-D-mannopyranoside, MANGANESE (II) ION, ... (6 entities in total)
Functional Keywordslectin, nonprotein amino acid, diocleinae, plant protein
Biological sourceCanavalia gladiata (Sword bean)
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Total number of polymer chains4
Total formula weight103822.56
Authors
Delatorre, P.,Rocha, B.A.M.,Souza, E.P.,Freitas, B.T.,Moreno, F.B.B.M.,Sampaio, A.H.,Azevedo Jr., W.F.,Cavada, B.S. (deposition date: 2005-11-19, release date: 2006-12-19, Last modification date: 2024-03-13)
Primary citationDelatorre, P.,Rocha, B.A.M.,Souza, E.P.,Oliveira, T.M.,Bezerra, G.A.,Moreno, F.B.M.B.,Freitas, B.T.,Santi-Gadelha, T.,Sampaio, A.H.,Azevedo Jr., W.F.,Cavada, B.S.
Structure of a lectin from Canavalia gladiata seeds: new structural insights for old molecules
Bmc Struct.Biol., 7:52-52, 2007
Cited by
PubMed Abstract: Lectins are mainly described as simple carbohydrate-binding proteins. Previous studies have tried to identify other binding sites, which possible recognize plant hormones, secondary metabolites, and isolated amino acid residues. We report the crystal structure of a lectin isolated from Canavalia gladiata seeds (CGL), describing a new binding pocket, which may be related to pathogen resistance activity in ConA-like lectins; a site where a non-protein amino-acid, alpha-aminobutyric acid (Abu), is bound.
PubMed: 17683532
DOI: 10.1186/1472-6807-7-52
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

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