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
Chain | GOid | namespace | contents |
A | 0006508 | biological_process | proteolysis |
A | 0008234 | molecular_function | cysteine-type peptidase activity |
B | 0006508 | biological_process | proteolysis |
B | 0008234 | molecular_function | cysteine-type peptidase activity |
C | 0006508 | biological_process | proteolysis |
C | 0008234 | molecular_function | cysteine-type peptidase activity |
D | 0006508 | biological_process | proteolysis |
D | 0008234 | molecular_function | cysteine-type peptidase activity |
I | 0001533 | cellular_component | cornified envelope |
I | 0002020 | molecular_function | protease binding |
I | 0004866 | molecular_function | endopeptidase inhibitor activity |
I | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
I | 0005515 | molecular_function | protein binding |
I | 0005615 | cellular_component | extracellular space |
I | 0005654 | cellular_component | nucleoplasm |
I | 0005737 | cellular_component | cytoplasm |
I | 0005829 | cellular_component | cytosol |
I | 0007155 | biological_process | cell adhesion |
I | 0018149 | biological_process | peptide cross-linking |
I | 0030216 | biological_process | keratinocyte differentiation |
I | 0030414 | molecular_function | peptidase inhibitor activity |
I | 0045861 | biological_process | negative regulation of proteolysis |
I | 0098609 | biological_process | cell-cell adhesion |
I | 1904090 | cellular_component | peptidase inhibitor complex |
J | 0001533 | cellular_component | cornified envelope |
J | 0002020 | molecular_function | protease binding |
J | 0004866 | molecular_function | endopeptidase inhibitor activity |
J | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
J | 0005515 | molecular_function | protein binding |
J | 0005615 | cellular_component | extracellular space |
J | 0005654 | cellular_component | nucleoplasm |
J | 0005737 | cellular_component | cytoplasm |
J | 0005829 | cellular_component | cytosol |
J | 0007155 | biological_process | cell adhesion |
J | 0018149 | biological_process | peptide cross-linking |
J | 0030216 | biological_process | keratinocyte differentiation |
J | 0030414 | molecular_function | peptidase inhibitor activity |
J | 0045861 | biological_process | negative regulation of proteolysis |
J | 0098609 | biological_process | cell-cell adhesion |
J | 1904090 | cellular_component | peptidase inhibitor complex |
K | 0001533 | cellular_component | cornified envelope |
K | 0002020 | molecular_function | protease binding |
K | 0004866 | molecular_function | endopeptidase inhibitor activity |
K | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
K | 0005515 | molecular_function | protein binding |
K | 0005615 | cellular_component | extracellular space |
K | 0005654 | cellular_component | nucleoplasm |
K | 0005737 | cellular_component | cytoplasm |
K | 0005829 | cellular_component | cytosol |
K | 0007155 | biological_process | cell adhesion |
K | 0018149 | biological_process | peptide cross-linking |
K | 0030216 | biological_process | keratinocyte differentiation |
K | 0030414 | molecular_function | peptidase inhibitor activity |
K | 0045861 | biological_process | negative regulation of proteolysis |
K | 0098609 | biological_process | cell-cell adhesion |
K | 1904090 | cellular_component | peptidase inhibitor complex |
L | 0001533 | cellular_component | cornified envelope |
L | 0002020 | molecular_function | protease binding |
L | 0004866 | molecular_function | endopeptidase inhibitor activity |
L | 0004869 | molecular_function | cysteine-type endopeptidase inhibitor activity |
L | 0005515 | molecular_function | protein binding |
L | 0005615 | cellular_component | extracellular space |
L | 0005654 | cellular_component | nucleoplasm |
L | 0005737 | cellular_component | cytoplasm |
L | 0005829 | cellular_component | cytosol |
L | 0007155 | biological_process | cell adhesion |
L | 0018149 | biological_process | peptide cross-linking |
L | 0030216 | biological_process | keratinocyte differentiation |
L | 0030414 | molecular_function | peptidase inhibitor activity |
L | 0045861 | biological_process | negative regulation of proteolysis |
L | 0098609 | biological_process | cell-cell adhesion |
L | 1904090 | cellular_component | peptidase inhibitor complex |
Functional Information from PROSITE/UniProt
site_id | PS00139 |
Number of Residues | 12 |
Details | THIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QGsCGSCWTfST |
Chain | Residue | Details |
A | GLN19-THR30 |
site_id | PS00287 |
Number of Residues | 14 |
Details | CYSTATIN Cysteine proteases inhibitors signature. TQVVAGTNYyIKVR |
Chain | Residue | Details |
I | THR52-ARG65 |
site_id | PS00639 |
Number of Residues | 11 |
Details | THIOL_PROTEASE_HIS Eukaryotic thiol (cysteine) proteases histidine active site. VNHAVLAVGYG |
Chain | Residue | Details |
A | VAL157-GLY167 |
site_id | PS00640 |
Number of Residues | 20 |
Details | THIOL_PROTEASE_ASN Eukaryotic thiol (cysteine) proteases asparagine active site. YWIvKNSWgpqWGmnGYFlI |
Chain | Residue | Details |
A | TYR170-ILE189 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | Active site: {} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 28 |
Details | Peptide: {"description":"Cathepsin H mini chain","featureId":"PRO_0000026219"} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 16 |
Details | Motif: {"description":"Secondary area of contact"} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Site: {"description":"Reactive site"} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"UniProtKB","id":"P01039","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | ASN175 | |
A | CYS25 | |
A | HIS159 |
site_id | CSA10 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | ASN175 | |
B | GLN19 | |
B | HIS159 |
site_id | CSA11 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
C | ASN175 | |
C | GLN19 | |
C | HIS159 |
site_id | CSA12 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
D | ASN175 | |
D | GLN19 | |
D | HIS159 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | ASN175 | |
B | CYS25 | |
B | HIS159 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
C | ASN175 | |
C | CYS25 | |
C | HIS159 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
D | ASN175 | |
D | CYS25 | |
D | HIS159 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | GLN19 | |
A | CYS25 | |
A | HIS159 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
B | GLN19 | |
B | CYS25 | |
B | HIS159 |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
C | GLN19 | |
C | CYS25 | |
C | HIS159 |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
D | GLN19 | |
D | CYS25 | |
D | HIS159 |
site_id | CSA9 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1pad |
Chain | Residue | Details |
A | ASN175 | |
A | GLN19 | |
A | HIS159 |
site_id | MCSA1 |
Number of Residues | |
Details | M-CSA 682 |
Chain | Residue | Details |
A | GLN19 | electrostatic stabiliser |
A | CYS25 | covalent catalysis, proton shuttle (general acid/base) |
A | HIS159 | electrostatic stabiliser, proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | |
Details | M-CSA 682 |
Chain | Residue | Details |
D | GLN19 | electrostatic stabiliser |
D | CYS25 | covalent catalysis, proton shuttle (general acid/base) |
D | HIS159 | electrostatic stabiliser, proton shuttle (general acid/base) |
site_id | MCSA3 |
Number of Residues | |
Details | M-CSA 682 |
Chain | Residue | Details |
site_id | MCSA4 |
Number of Residues | |
Details | M-CSA 682 |
Chain | Residue | Details |
J | VAL25 | electrostatic stabiliser |
J | GLN31 | covalent catalysis, proton shuttle (general acid/base) |