Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 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 E 501 |
| Chain | Residue |
| E | GLN2 |
| E | ASP41 |
| E | LEU75 |
| E | ASN77 |
| E | ILE79 |
| E | VAL81 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE CA E 502 |
| Chain | Residue |
| E | GLY169 |
| E | LYS170 |
| E | TYR171 |
| E | VAL174 |
| E | GLU195 |
| E | ASP197 |
| E | HOH631 |
| E | HOH632 |
| site_id | CAT |
| Number of Residues | 3 |
| Details | RESIDUES FORMING THE CATALYTIC TRIAD IN SUBTILISIN |
| Chain | Residue |
| E | ASP32 |
| E | HIS64 |
| E | SER221 |
| site_id | RAC |
| Number of Residues | 2 |
| Details | TWO RESIDUES OF SSI CONNECTED THROUGH A REACTIVE SITE PEPTIDE BOND (OR A SCISSIBLE BOND) WHICH IS POTENTIALLY CLEAVED BY TARGET ENZYMES INCLUDING SUBTILISIN |
| site_id | S13 |
| Number of Residues | 3 |
| Details | S1-3 SITE, COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT OF SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P1, P2 AND P3 RESIDUES OF A LIGAND |
| Chain | Residue |
| E | SER125 |
| E | LEU126 |
| E | GLY127 |
| site_id | S46 |
| Number of Residues | 3 |
| Details | S4-6 SITE AND COMPRISES A THREE-RESIDUE POLYPEPTIDE SEGMENT OF SUBTILISIN CAPABLE OF FORMING AN ANTIPARALLEL BETA-SHEET WITH THE P4, P5 AND P6 RESIDUES OF A LIGAND |
| Chain | Residue |
| E | GLY102 |
| E | GLN103 |
| E | TYR104 |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VAVIDSGIdssH |
| Chain | Residue | Details |
| E | VAL28-HIS39 | |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGThVAGtVAA |
| Chain | Residue | Details |
| E | HIS64-ALA74 | |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSmAsPhVAG |
| Chain | Residue | Details |
| E | GLY219-GLY229 | |
| site_id | PS00999 |
| Number of Residues | 19 |
| Details | SSI Streptomyces subtilisin-type inhibitors signature. CaPgpsGtHPaagsACAdL |
| Chain | Residue | Details |
| I | CYS35-LEU53 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 269 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"5249818","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Repeat: {} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond for subtilisin"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| E | SER221 | |
| E | HIS64 | |
| E | ASP32 | |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 723 |
