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 |
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 | 4 |
Details | BINDING SITE FOR RESIDUE DIO A 368 |
Chain | Residue |
A | ASN62 |
A | HIS64 |
A | TYR209 |
A | LEU217 |
site_id | ACT |
Number of Residues | 3 |
Details | |
Chain | Residue |
A | ASP32 |
A | HIS64 |
A | SER221 |
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 | 268 |
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"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 9 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"8512925","evidenceCode":"ECO:0000269"}]} |
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 | |