2D7F
Crystal structure of A lectin from canavalia gladiata seeds complexed with alpha-methyl-mannoside and alpha-aminobutyric acid
Summary for 2D7F
Entry DOI | 10.2210/pdb2d7f/pdb |
Related | 1WUV |
Descriptor | Concanavalin A, methyl alpha-D-mannopyranoside, MANGANESE (II) ION, ... (6 entities in total) |
Functional Keywords | lectin, nonprotein amino acid, diocleinae, plant protein |
Biological source | Canavalia gladiata (Sword bean) More |
Total number of polymer chains | 4 |
Total formula weight | 103822.56 |
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 citation | Delatorre, 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: 17683532DOI: 10.1186/1472-6807-7-52 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.31 Å) |
Structure validation
Download full validation report