Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3KFQ

Unreduced cathepsin V in complex with stefin A

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
C0001533cellular_componentcornified envelope
C0002020molecular_functionprotease binding
C0004866molecular_functionendopeptidase inhibitor activity
C0004869molecular_functioncysteine-type endopeptidase inhibitor activity
C0005515molecular_functionprotein binding
C0005615cellular_componentextracellular space
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0007155biological_processcell adhesion
C0018149biological_processpeptide cross-linking
C0030216biological_processkeratinocyte differentiation
C0030414molecular_functionpeptidase inhibitor activity
C0045861biological_processnegative regulation of proteolysis
C0098609biological_processcell-cell adhesion
C1904090cellular_componentpeptidase inhibitor complex
D0001533cellular_componentcornified envelope
D0002020molecular_functionprotease binding
D0004866molecular_functionendopeptidase inhibitor activity
D0004869molecular_functioncysteine-type endopeptidase inhibitor activity
D0005515molecular_functionprotein binding
D0005615cellular_componentextracellular space
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0007155biological_processcell adhesion
D0018149biological_processpeptide cross-linking
D0030216biological_processkeratinocyte differentiation
D0030414molecular_functionpeptidase inhibitor activity
D0045861biological_processnegative regulation of proteolysis
D0098609biological_processcell-cell adhesion
D1904090cellular_componentpeptidase inhibitor complex
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QKqCGSCWAfSA
ChainResidueDetails
AGLN19-ALA30

site_idPS00287
Number of Residues14
DetailsCYSTATIN Cysteine proteases inhibitors signature. TQVVAGTNYyIKVR
ChainResidueDetails
CTHR45-ARG58

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. LDHGVLVVGYG
ChainResidueDetails
ALEU162-GLY172

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvKNSWgpeWGsnGYVkI
ChainResidueDetails
ATYR183-ILE202

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11027133","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"22967898","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsMotif: {"description":"Secondary area of contact"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Reactive site"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P01039","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

244349

PDB entries from 2025-11-05

PDB statisticsPDBj update infoContact PDBjnumon