1dq0 Summary


Locked, metal-free concanavalin A, a minor species in solution

The structure was published by Bouckaert, J., Dewallef, Y., Poortmans, F., Wyns, L., and Loris, R., in 2000 in a paper entitled "The structural features of concanavalin A governing non-proline peptide isomerization" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 1999.

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

The PDB entry contains the structure of LOCKED METAL-FREE CONCANAVALIN A. This molecule has the UniProt identifier P02866 (CONA_CANEN)search. The sample contained 237 residues which is < 90% of the natural sequence. Out of 237 residues 237 were observed and are deposited in the PDB.

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 LOCKED METAL-FREE CONCANAVALIN A P02866 (28-148) (CONA_CANEN)search Canavalia ensiformissearch 91% 237 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P02866 (28 - 148) LOCKED METAL-FREE CONCANAVALIN A Canavalia ensiformis

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P02866) Legume lectinssearch Jelly Rollssearch PF00139: Legume lectin domainsearch

Chain ID Molecular function (GO)
A (P02866) carbohydrate bindingsearch

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