7pck Summary



The structure was published by Sivaraman, J., Lalumiere, M., Menard, R., and Cygler, M., in 1999 in a paper entitled "Crystal structure of wild-type human procathepsin K." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.2 Å and deposited in 1998.

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

This PDB entry contains multiple copies of the structure of PROTEIN (PROCATHEPSIN K).

The molecule most likely forms homotetramers.

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 PROTEIN (PROCATHEPSIN K) P43235 (16-329) (CATK_HUMAN)search Homo sapienssearch 100% 314 100%
B PROTEIN (PROCATHEPSIN K) P43235 (16-329) (CATK_HUMAN)search Homo sapienssearch 100% 314 100%
C PROTEIN (PROCATHEPSIN K) P43235 (16-329) (CATK_HUMAN)search Homo sapienssearch 100% 314 100%
D PROTEIN (PROCATHEPSIN K) P43235 (16-329) (CATK_HUMAN)search Homo sapienssearch 100% 314 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P43235 (16 - 329) PROTEIN (PROCATHEPSIN K) Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B, C, D (P43235) Papain-likesearch Cysteine proteinasessearch PF00112: Papain family cysteine proteasesearch, PF08246: Cathepsin propeptide inhibitor domain (I29)search

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A, B, C, D (P43235) bone resorptionsearch intramembranous ossificationsearch collagen catabolic processsearch proteolysissearch extracellular matrix disassemblysearch proteolysis involved in cellular protein catabolic processsearch extracellular matrix organizationsearch toll-like receptor signaling pathwaysearch innate immune responsesearch hydrolase activitysearch peptidase activitysearch cysteine-type peptidase activitysearch cysteine-type endopeptidase activitysearch collagen bindingsearch fibronectin bindingsearch proteoglycan bindingsearch lysosomesearch cytoplasmsearch extracellular regionsearch extracellular spacesearch endolysosome lumensearch

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