Activated Toxoplasma gondii cathepsin L (TgCPL) in complex with its propeptide
The structure was published by Larson, E.T., Parussini, F., Huynh, M.H., et al., Bogyo, M., Merritt, E.A., and Carruthers, V.B., in 2009 in a paper entitled "Toxoplasma gondii cathepsin L is the primary target of the invasion-inhibitory compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.99 Å and deposited in 2008.
The experimental data on which the structure is based was also deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Cathepsin L Protease and Cathepsin L Propeptide.
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 heterodimers.
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: