X-RAY CRYSTAL STRUCTURE DETERMINATION AND REFINEMENT AT 1.9 ANGSTROMS RESOLUTION OF ISOLECTIN I FROM THE SEEDS OF LATHYRUS OCHRUS
The structure was published by Bourne, Y., Abergel, C., Cambillau, C., Frey, M., Rouge, P., and Fontecilla-Camps, J.C., in 1990 in a paper entitled "X-ray crystal structure determination and refinement at 1.9 A resolution of isolectin I from the seeds of Lathyrus ochrus." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1993.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely LEGUME ISOLECTIN I (ALPHA CHAIN) and LEGUME ISOLECTIN I (BETA CHAIN).
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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 2 unique UniProt proteins: