Cathepsin K covalently bound to a cyano-pyrimidine inhibitor with improved selectivity over hERG
The structure was published by Rankovic, Z., Cai, J., Kerr, J., et al., Deronzier, H., Dorleans, C., and Nicolai, E., in 2010 in a paper entitled "Optimisation of 2-cyano-pyrimidine inhibitors of cathepsin K: improving selectivity over hERG." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 2010.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Cathepsin K. This molecule has the UniProt identifier P43235 (CATK_HUMAN). The sample contained 215 residues which is < 90% of the natural sequence. Out of 215 residues 215 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 is most likely monomeric.
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: