1cjl Summary



The structure was published by Coulombe, R., Grochulski, P., Sivaraman, J., Menard, R., Mort, J.S., and Cygler, M., in 1996 in a paper entitled "Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegment." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1996.

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

The PDB entry contains the structure of PROCATHEPSIN L. This molecule has the UniProt identifier P07711 (CATL1_HUMAN)search. The sample contained 312 residues which is 99% of the natural sequence. Out of 312 residues 307 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 L P07711 (22-333) (CATL1_HUMAN)search Homo sapienssearch 99% 312 98%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P07711 (22 - 333) PROCATHEPSIN L Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (P07711) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch, PF08246: Cathepsin propeptide inhibitor domain (I29)search

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P07711) protein bindingsearch proteoglycan bindingsearch collagen bindingsearch cysteine-type peptidase activitysearch fibronectin bindingsearch peptidase activitysearch cysteine-type endopeptidase activitysearch hydrolase activitysearch histone bindingsearch extracellular matrix disassemblysearch collagen catabolic processsearch proteolysissearch toll-like receptor signaling pathwaysearch antigen processing and presentation of exogenous peptide antigen via MHC class IIsearch extracellular matrix organizationsearch adaptive immune responsesearch macrophage apoptotic processsearch antigen processing and presentationsearch proteolysis involved in cellular protein catabolic processsearch cellular response to thyroid hormone stimulussearch innate immune responsesearch extracellular spacesearch extracellular vesicular exosomesearch endolysosome lumensearch extracellular regionsearch lysosomal lumensearch lysosomesearch nucleussearch

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