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The Crystal Structure of Canavalia Maritima Lectin (ConM) in Complex with Trehalose and Maltose

The structure was published by Delatorre, P., Rocha, B.A.M., Gadelha, C.A.A., et al., Sampaio, A.H., Azevedo Jr., W.F., and Cavada, B.S., in 2006 in a paper entitled "Crystal structure of a lectin from Canavalia maritima (ConM) in complex with trehalose and maltose reveals relevant mutation in ConA-like lectins" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Lectin.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Lectin P55915 (1-237) (CONA_CANBR)search Canavalia brasiliensissearch 100% 237 97%
C Lectin Not available
Canavalia roseasearch 100% 237 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P55915 (1 - 237) Lectin Canavalia rosea

Chain Structural classification (CATH) Sequence family (Pfam)
A, C (P55915) Jelly Rollssearch PF00139: Legume lectin domainsearch

Chain ID Molecular function (GO)
A, C (P55915) carbohydrate bindingsearch mannose bindingsearch metal ion bindingsearch

Chain InterPro annotation
A, C Legume lectin, alpha chain, conserved sitesearch Legume lectin domainsearch search Concanavalin A-like lectin/glucanase domainsearch Legume lectin, beta chain, Mn/Ca-binding sitesearch