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 | 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 |
| 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 | 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 |
| 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 | 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 |
| 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 | 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 |
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) |
