CRYSTAL STRUCTURE OF THE SOYBEAN AGGLUTININ IN A COMPLEX WITH A BIANTENNARY BLOOD GROUP ANTIGEN ANALOG
The structure was published by Buts, L., Dao-Thi, M.H., Loris, R., Wyns, L., Etzler, M., and Hamelryck, T., in 2001 in a paper entitled "Weak protein-protein interactions in lectins: the crystal structure of a vegetative lectin from the legume Dolichos biflorus." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2000.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of LECTIN. This molecule has the UniProt identifier P05046 (LEC_SOYBN). The sample contained 253 residues which is 100% of the natural sequence. Out of 253 residues 232 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):
This entry contains 1 unique UniProt protein: