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1BY8

THE CRYSTAL STRUCTURE OF HUMAN PROCATHEPSIN K

Functional Information from GO Data
ChainGOidnamespacecontents
A0000423biological_processmitophagy
A0001968molecular_functionfibronectin binding
A0004197molecular_functioncysteine-type endopeptidase activity
A0004252molecular_functionserine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005518molecular_functioncollagen binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0006508biological_processproteolysis
A0006590biological_processthyroid hormone generation
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0009897cellular_componentexternal side of plasma membrane
A0016324cellular_componentapical plasma membrane
A0016787molecular_functionhydrolase activity
A0022617biological_processextracellular matrix disassembly
A0030574biological_processcollagen catabolic process
A0036021cellular_componentendolysosome lumen
A0043202cellular_componentlysosomal lumen
A0043394molecular_functionproteoglycan binding
A0051603biological_processproteolysis involved in protein catabolic process
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGqCGSCWAfSS
ChainResidueDetails
AGLN118-SER129

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LNHAVLAVGYG
ChainResidueDetails
ALEU259-GLY269

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. HWIiKNSWgenWGnkGYIlM
ChainResidueDetails
AHIS276-MET295

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AASN281
ACYS124
AHIS261

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN118
ACYS124
AHIS261

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN118
AASN281
AHIS261

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PDB entries from 2025-12-17

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