1i3h Summary



The structure was published by Sanders, D.A., Moothoo, D.N., Raftery, J., Howard, A.J., Helliwell, J.R., and Naismith, J.H., in 2001 in a paper entitled "The 1.2 A resolution structure of the Con A-dimannose complex." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.2 Å and deposited in 2001.

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

The PDB entry contains the structure of 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.

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 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) 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 search Concanavalin A-like lectin/glucanase domainsearch Legume lectin, beta chain, Mn/Ca-binding sitesearch