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1JQP

dipeptidyl peptidase I (cathepsin C), a tetrameric cysteine protease of the papain family

Functional Information from GO Data
ChainGOidnamespacecontents
A0001913biological_processT cell mediated cytotoxicity
A0004197molecular_functioncysteine-type endopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005615cellular_componentextracellular space
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005813cellular_componentcentrosome
A0006508biological_processproteolysis
A0006915biological_processapoptotic process
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0008239molecular_functiondipeptidyl-peptidase activity
A0016505molecular_functionpeptidase activator activity involved in apoptotic process
A0016787molecular_functionhydrolase activity
A0019902molecular_functionphosphatase binding
A0031404molecular_functionchloride ion binding
A0031642biological_processnegative regulation of myelination
A0042802molecular_functionidentical protein binding
A0043231cellular_componentintracellular membrane-bounded organelle
A0051087molecular_functionprotein-folding chaperone binding
A0051603biological_processproteolysis involved in protein catabolic process
A1903052biological_processpositive regulation of proteolysis involved in protein catabolic process
A1903980biological_processpositive regulation of microglial cell activation
A2001235biological_processpositive regulation of apoptotic signaling pathway
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QEsCGSCYSfAS
ChainResidueDetails
AGLN227-SER238

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. TNHAVLLVGYG
ChainResidueDetails
ATHR378-GLY388

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWgsqWGesGYFrI
ChainResidueDetails
ATYR397-ILE416

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10088
ChainResidueDetails
ACYS233

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10089
ChainResidueDetails
AHIS380

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU10090
ChainResidueDetails
AASN402

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P53634
ChainResidueDetails
APHE277
ATYR279
ATYR322

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11602245
ChainResidueDetails
AASN5
AASN251

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN29
AASN120

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
ACYS233
AHIS380
AASN402

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS380
ACYS233
AGLN227

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS380
AASN402
AGLN227

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PDB entries from 2025-06-11

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