3kfq Summary

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Unreduced cathepsin V in complex with stefin A

A publication describing this structure is not available. The depositing authors are Renko, M.search; Turk, D.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.99 Å and deposited in 2009.

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

This PDB entry contains a complex of 2 biomacromolecules, namely Cathepsin L2 and Cystatin-A.

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 L2 O60911 (114-334) (CATL2_HUMAN)search Homo sapienssearch < 90% 221 100%
B Cathepsin L2 O60911 (114-334) (CATL2_HUMAN)search Homo sapienssearch < 90% 221 100%
C Cystatin-A P01040 (1-98) (CYTA_HUMAN)search Homo sapienssearch 100% 98 100%
D Cystatin-A P01040 (1-98) (CYTA_HUMAN)search Homo sapienssearch 100% 98 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
O60911 (114 - 334) Cathepsin L2 Homo sapiens
P01040 (1 - 98) Cystatin-A Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Cysteine proteinasessearch Papain family cysteine proteasesearch
C, D (P01040) PF00031: Cystatin domainsearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A, B (O60911) cysteine-type peptidase activitysearch proteolysissearch
C, D (P01040) endopeptidase inhibitor activitysearch cysteine-type endopeptidase inhibitor activitysearch protein binding, bridgingsearch structural molecule activitysearch protease bindingsearch peptidase inhibitor activitysearch negative regulation of endopeptidase activitysearch negative regulation of proteolysissearch single organismal cell-cell adhesionsearch keratinocyte differentiationsearch negative regulation of peptidase activitysearch peptide cross-linkingsearch cell adhesionsearch intracellularsearch cytoplasmsearch cornified envelopesearch extracellular vesicular exosomesearch nucleussearch extracellular spacesearch

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
C, D Proteinase inhibitor I25, cystatinsearch Proteinase inhibitor I25A, stefin Asearch Proteinase inhibitor I25, cystatin, conserved sitesearch