CRYSTAL STRUCTURE OF THE CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT PYRROLIDINONE INHIBITOR
The structure was published by Marquis, R.W., Yamashita, D.S., Ru, Y., et al., Tomaszek, T.A., Levy, M.A., and Veber, D.F., in 1998 in a paper entitled "Conformationally constrained 1,3-diamino ketones: a series of potent inhibitors of the cysteine protease cathepsin K." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 1997.
The experimental data on which the structure is based was not 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: