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2C0Y

THE CRYSTAL STRUCTURE OF A CYS25ALA MUTANT OF HUMAN PROCATHEPSIN S

Functional Information from GO Data
ChainGOidnamespacecontents
A0001968molecular_functionfibronectin binding
A0002224biological_processtoll-like receptor signaling pathway
A0002250biological_processadaptive immune response
A0002577biological_processregulation of antigen processing and presentation
A0004197molecular_functioncysteine-type endopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0005770cellular_componentlate endosome
A0006508biological_processproteolysis
A0006955biological_processimmune response
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0010447biological_processresponse to acidic pH
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0019882biological_processantigen processing and presentation
A0019886biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II
A0022617biological_processextracellular matrix disassembly
A0030574biological_processcollagen catabolic process
A0031012cellular_componentextracellular matrix
A0031410cellular_componentcytoplasmic vesicle
A0034769biological_processbasement membrane disassembly
A0036021cellular_componentendolysosome lumen
A0043202cellular_componentlysosomal lumen
A0043236molecular_functionlaminin binding
A0043394molecular_functionproteoglycan binding
A0045335cellular_componentphagocytic vesicle
A0048002biological_processantigen processing and presentation of peptide antigen
A0051603biological_processproteolysis involved in protein catabolic process
A0097067biological_processcellular response to thyroid hormone stimulus
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
A2001259biological_processpositive regulation of cation channel activity
Functional Information from PROSITE/UniProt
site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHGVLVVGYG
ChainResidueDetails
AVAL261-GLY271

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWghnFGeeGYIrM
ChainResidueDetails
ATYR278-MET297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
AALA124
AHIS263
AASN283

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:9524075
ChainResidueDetails
AASN89

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
AGLN118
AASN283
AHIS263

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 9pap
ChainResidueDetails
AGLN118
AHIS263
AASN283
AALA124

site_idMCSA1
Number of Residues4
DetailsM-CSA 814
ChainResidueDetails
AGLN118electrostatic stabiliser
AALA124nucleofuge, nucleophile, proton acceptor, proton donor
AHIS263proton acceptor, proton donor
AASN283electrostatic stabiliser

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PDB entries from 2025-06-18

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