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3K9M

Cathepsin B 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
C0010466biological_processnegative regulation of peptidase activity
C0018149biological_processpeptide cross-linking
C0030216biological_processkeratinocyte differentiation
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
D0010466biological_processnegative regulation of peptidase activity
D0018149biological_processpeptide cross-linking
D0030216biological_processkeratinocyte differentiation
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. QGsCGSCWAfGA
ChainResidueDetails
AGLN23-ALA34

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. GGHAIRILGWG
ChainResidueDetails
AGLY197-GLY207

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWLvANSWntdWGdnGFFkI
ChainResidueDetails
ATYR214-ILE233

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Reactive site
ChainResidueDetails
CGLY4
DGLY4
AASN219
BCYS29
BHIS199
BASN219

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000250|UniProtKB:P01039
ChainResidueDetails
CMET1
DMET1

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3463996
ChainResidueDetails
AASN113
BASN113

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS199
AASN219
ACYS29

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS199
BASN219
BCYS29

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS199
AGLN23
ACYS29

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS199
BGLN23
BCYS29

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AHIS199
AASN219
AGLN23

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BHIS199
BASN219
BGLN23

224004

PDB entries from 2024-08-21

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