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

1NB3

Crystal structure of stefin A in complex with cathepsin H: N-terminal residues of inhibitors can adapt to the active sites of endo-and exopeptidases

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
D0006508biological_processproteolysis
D0008234molecular_functioncysteine-type peptidase activity
I0001533cellular_componentcornified envelope
I0002020molecular_functionprotease binding
I0004866molecular_functionendopeptidase inhibitor activity
I0004869molecular_functioncysteine-type endopeptidase inhibitor activity
I0005515molecular_functionprotein binding
I0005615cellular_componentextracellular space
I0005654cellular_componentnucleoplasm
I0005737cellular_componentcytoplasm
I0005829cellular_componentcytosol
I0007155biological_processcell adhesion
I0018149biological_processpeptide cross-linking
I0030216biological_processkeratinocyte differentiation
I0030414molecular_functionpeptidase inhibitor activity
I0045861biological_processnegative regulation of proteolysis
I0098609biological_processcell-cell adhesion
I1904090cellular_componentpeptidase inhibitor complex
J0001533cellular_componentcornified envelope
J0002020molecular_functionprotease binding
J0004866molecular_functionendopeptidase inhibitor activity
J0004869molecular_functioncysteine-type endopeptidase inhibitor activity
J0005515molecular_functionprotein binding
J0005615cellular_componentextracellular space
J0005654cellular_componentnucleoplasm
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0007155biological_processcell adhesion
J0018149biological_processpeptide cross-linking
J0030216biological_processkeratinocyte differentiation
J0030414molecular_functionpeptidase inhibitor activity
J0045861biological_processnegative regulation of proteolysis
J0098609biological_processcell-cell adhesion
J1904090cellular_componentpeptidase inhibitor complex
K0001533cellular_componentcornified envelope
K0002020molecular_functionprotease binding
K0004866molecular_functionendopeptidase inhibitor activity
K0004869molecular_functioncysteine-type endopeptidase inhibitor activity
K0005515molecular_functionprotein binding
K0005615cellular_componentextracellular space
K0005654cellular_componentnucleoplasm
K0005737cellular_componentcytoplasm
K0005829cellular_componentcytosol
K0007155biological_processcell adhesion
K0018149biological_processpeptide cross-linking
K0030216biological_processkeratinocyte differentiation
K0030414molecular_functionpeptidase inhibitor activity
K0045861biological_processnegative regulation of proteolysis
K0098609biological_processcell-cell adhesion
K1904090cellular_componentpeptidase inhibitor complex
L0001533cellular_componentcornified envelope
L0002020molecular_functionprotease binding
L0004866molecular_functionendopeptidase inhibitor activity
L0004869molecular_functioncysteine-type endopeptidase inhibitor activity
L0005515molecular_functionprotein binding
L0005615cellular_componentextracellular space
L0005654cellular_componentnucleoplasm
L0005737cellular_componentcytoplasm
L0005829cellular_componentcytosol
L0007155biological_processcell adhesion
L0018149biological_processpeptide cross-linking
L0030216biological_processkeratinocyte differentiation
L0030414molecular_functionpeptidase inhibitor activity
L0045861biological_processnegative regulation of proteolysis
L0098609biological_processcell-cell adhesion
L1904090cellular_componentpeptidase inhibitor complex
Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWTfST
ChainResidueDetails
AGLN19-THR30

site_idPS00287
Number of Residues14
DetailsCYSTATIN Cysteine proteases inhibitors signature. TQVVAGTNYyIKVR
ChainResidueDetails
ITHR52-ARG65

site_idPS00639
Number of Residues11
DetailsTHIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHAVLAVGYG
ChainResidueDetails
AVAL157-GLY167

site_idPS00640
Number of Residues20
DetailsTHIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWgpqWGmnGYFlI
ChainResidueDetails
ATYR170-ILE189

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsPeptide: {"description":"Cathepsin H mini chain","featureId":"PRO_0000026219"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsMotif: {"description":"Secondary area of contact"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsSite: {"description":"Reactive site"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsModified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P01039","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AASN175
ACYS25
AHIS159

site_idCSA10
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BASN175
BGLN19
BHIS159

site_idCSA11
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
CASN175
CGLN19
CHIS159

site_idCSA12
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
DASN175
DGLN19
DHIS159

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BASN175
BCYS25
BHIS159

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
CASN175
CCYS25
CHIS159

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
DASN175
DCYS25
DHIS159

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AGLN19
ACYS25
AHIS159

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
BGLN19
BCYS25
BHIS159

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
CGLN19
CCYS25
CHIS159

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
DGLN19
DCYS25
DHIS159

site_idCSA9
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pad
ChainResidueDetails
AASN175
AGLN19
AHIS159

site_idMCSA1
Number of Residues
DetailsM-CSA 682
ChainResidueDetails
AGLN19electrostatic stabiliser
ACYS25covalent catalysis, proton shuttle (general acid/base)
AHIS159electrostatic stabiliser, proton shuttle (general acid/base)

site_idMCSA2
Number of Residues
DetailsM-CSA 682
ChainResidueDetails
DGLN19electrostatic stabiliser
DCYS25covalent catalysis, proton shuttle (general acid/base)
DHIS159electrostatic stabiliser, proton shuttle (general acid/base)

site_idMCSA3
Number of Residues
DetailsM-CSA 682
ChainResidueDetails

site_idMCSA4
Number of Residues
DetailsM-CSA 682
ChainResidueDetails
JVAL25electrostatic stabiliser
JGLN31covalent catalysis, proton shuttle (general acid/base)

238895

PDB entries from 2025-07-16

PDB statisticsPDBj update infoContact PDBjnumon