1ayv Summary

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CRYSTAL STRUCTURE OF CYSTEINE PROTEASE HUMAN CATHEPSIN K IN COMPLEX WITH A COVALENT THIAZOLHYDRAZIDE INHIBITOR

The structure was published by Thompson, S.K., Halbert, S.M., Bossard, M.J., et al., Gowen, M., Gleason, J.G., and Veber, D.F., in 1997 in a paper entitled "Design of potent and selective human cathepsin K inhibitors that span the active site." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 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)search. 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):


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 (115-329) (CATK_HUMAN)search Homo sapienssearch 100% 215 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P43235 (115 - 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