REFINEMENT OF TWO CRYSTAL FORMS OF LENTIL LECTIN AT 1.8 ANGSTROMS RESOLUTION
The structure was published by Loris, R., Van Overberge, D., Dao-Thi, M.H., Poortmans, F., Maene, N., and Wyns, L., in 1994 in a paper entitled "Structural analysis of two crystal forms of lentil lectin at 1.8 A resolution." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1993.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely 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 heterotetramers.
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: