1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR019825 | Binding_site | Legume lectin, beta chain, Mn/Ca-binding site |
1 Parent Features
| DB identifier | Type | Name |
|---|---|---|
| IPR013320 | Domain | Concanavalin A-like lectin/glucanase domain |
| Type: | Domain | Name: | Legume lectin domain |
| Description: | Lectins are carbohydrate-binding proteins. Leguminous lectins form one of the largest lectin families and resemble each other in their physicochemical properties, though they differ in their carbohydrate specificities. They bind either glucose/mannose or galactose []. Carbohydrate-binding activity depends on the simultaneous presence of both acalcium and a transition metal ion []. The exact function of legume lectins is not known, but they may be involved in the attachment of nitrogen-fixing bacteria to legumes and in the protection against pathogens [, ].Some legume lectins are proteolytically processed to produce two chains, beta (which corresponds to the N-terminal) and alpha (C-terminal) []. The lectin concanavalin A (conA) from jack bean is exceptional in that the two chains are transposed and ligated (by formation of a new peptide bond). The N terminus of mature conA thus corresponds to that of the alpha chain and the C terminus to the beta chain []. Though the legume lectins monomer is structurally well conserved, their quaternary structures vary widely []. | Short Name: | Legume_lectin_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR019825 | Binding_site | Legume lectin, beta chain, Mn/Ca-binding site |
| DB identifier | Type | Name |
|---|---|---|
| IPR013320 | Domain | Concanavalin A-like lectin/glucanase domain |
