Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| I | 0005576 | cellular_component | extracellular region |
| I | 0030414 | molecular_function | peptidase inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 276 |
| Chain | Residue |
| A | GLN2 |
| A | ASP41 |
| A | LEU75 |
| A | ASN77 |
| A | THR79 |
| A | VAL81 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA B 276 |
| Chain | Residue |
| B | ASN77 |
| B | THR79 |
| B | VAL81 |
| B | GLN2 |
| B | ASP41 |
| B | LEU75 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVLDTGIqasH |
| Chain | Residue | Details |
| A | VAL28-HIS39 | |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA |
| Chain | Residue | Details |
| A | HIS64-ALA74 | |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG |
| Chain | Residue | Details |
| A | GLY219-GLY229 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 536 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"8512925","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 55 |
| Details | Repeat: {"description":"1; trypsin-inhibitory"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond for trypsin"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond for chymotrypsin"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| A | SER221 | |
| A | HIS64 | |
| A | ASP32 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| B | SER221 | |
| B | HIS64 | |
| B | ASP32 | |
