Crystal structure of recombinant barley cysteine endoprotease B isoform 2 (EP-B2) in complex with leupeptin
The structure was published by Bethune, M.T., Strop, P., Tang, Y., Sollid, L.M., and Khosla, C., in 2006 in a paper entitled "Heterologous Expression, Purification, Refolding, and Structural-Functional Characterization of EP-B2, a Self-Activating Barley Cysteine Endoprotease." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2006.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Cysteine proteinase EP-B 2 and ACE-LEU-LEU-argininal (leupeptin).
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 1 unique UniProt protein: