2c0y Summary



The structure was published by Kaulmann, G., Palm, G.J., Schilling, K., Hilgenfeld, R., and Wiederanders, B., in 2006 in a paper entitled "The Crystal Structure of a Cys25 -> Ala Mutant of Human Procathepsin S Elucidates Enzyme-Prosequence Interactions." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.1 Å and deposited in 2005.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of PROCATHEPSIN S. This molecule has the UniProt identifier P25774 (CATS_HUMAN)search. The sample contained 315 residues which is 100% of the natural sequence. Out of 315 residues 308 were observed and are deposited in the PDB.

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 PROCATHEPSIN S P25774 (17-331) (CATS_HUMAN)search Homo sapienssearch 100% 315 97%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P25774 (17 - 331) PROCATHEPSIN S Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A (P25774) Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch, PF08246: Cathepsin propeptide inhibitor domain (I29)search

Chain ID Biological process (GO) Cellular component (GO) Molecular function (GO)
A (P25774) cellular response to thyroid hormone stimulussearch antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-independentsearch antigen processing and presentationsearch extracellular matrix organizationsearch collagen catabolic processsearch immune responsesearch proteolysissearch adaptive immune responsesearch extracellular matrix disassemblysearch positive regulation of inflammatory responsesearch antigen processing and presentation of exogenous peptide antigen via MHC class IIsearch antigen processing and presentation of peptide antigen via MHC class Isearch antigen processing and presentation of exogenous peptide antigen via MHC class Isearch basement membrane disassemblysearch toll-like receptor signaling pathwaysearch innate immune responsesearch proteolysis involved in cellular protein catabolic processsearch membranesearch endolysosome lumensearch lysosomal lumensearch lysosomesearch intracellular membrane-bounded organellesearch extracellular regionsearch extracellular spacesearch peptidase activitysearch laminin bindingsearch hydrolase activitysearch cysteine-type endopeptidase activitysearch fibronectin bindingsearch cysteine-type peptidase activitysearch collagen bindingsearch proteoglycan bindingsearch

Chain InterPro annotation
A Peptidase C1A, papain C-terminalsearch Peptidase C1Asearch Proteinase inhibitor I29, cathepsin propeptidesearch Cysteine peptidase, histidine active sitesearch Cysteine peptidase, asparagine active sitesearch