1u9v Summary


Crystal Structure of the Cysteine Protease Human Cathepsin K in Complex with the Covalent Inhibitor NVP-ABE854

The structure was published by Altmann, E., Cowan-Jacob, S.W., and Missbach, M., in 2004 in a paper entitled "Novel purine nitrile derived inhibitors of the cysteine protease cathepsin K" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2004.

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)search. The sample contained 217 residues which is < 90% of the natural sequence. Out of 217 residues 213 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Cathepsin K P43235 (113-329) (CATK_HUMAN)search Homo sapienssearch 100% 217 99%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P43235 (113 - 329) Cathepsin K Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P43235) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P43235) cysteine-type peptidase activitysearch proteolysissearch

Chain InterPro annotation
A Cysteine peptidase, cysteine active sitesearch Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Peptidase C1A, cathepsin Ksearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch