2op3 Summary


The structure of cathepsin S with a novel 2-arylphenoxyacetaldehyde inhibitor derived by the Substrate Activity Screening (SAS) method

The structure was published by Inagaki, H., Tsuruoka, H., Hornsby, M., Lesley, S.A., Spraggon, G., and Ellman, J.A., in 2007 in a paper entitled "Characterization and optimization of selective, nonpeptidic inhibitors of cathepsin S with an unprecedented binding mode." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.6 Å and deposited in 2007.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of Cathepsin S.

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 has more than one probable quaternary state observed. For more details see the quaternary structure page.

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 S P25774 (112-331) (CATS_HUMAN)search Homo sapienssearch 100% 220 98%
B Cathepsin S P25774 (112-331) (CATS_HUMAN)search Homo sapienssearch 100% 220 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P25774 (112 - 331) Cathepsin S Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (P25774) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P25774) cysteine-type peptidase activitysearch proteolysissearch

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