Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0004252 | molecular_function | serine-type endopeptidase activity |
E | 0006508 | biological_process | proteolysis |
I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAGHC |
Chain | Residue | Details |
E | LEU53-CYS58 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. CAepGDSGGPLY |
Chain | Residue | Details |
E | CYS191-TYR200 | |
site_id | PS00282 |
Number of Residues | 23 |
Details | KAZAL_1 Kazal serine protease inhibitors family signature. CtieyRplCgSdnktYgnkCnf.C |
Chain | Residue | Details |
I | CYS16-CYS38 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Reactive bond 3 for chymotrypsin, elastase, proteases A and B, and subtilisin |
Chain | Residue | Details |
I | ILE18 | |
E | ASP102 | |
E | SER195 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine |
Chain | Residue | Details |
I | ASN45 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1ssx |
Chain | Residue | Details |
E | ASP102 | |
E | SER195 | |
E | GLY193 | |
E | HIS57 | |
site_id | CSA2 |
Number of Residues | 5 |
Details | Annotated By Reference To The Literature 1ssx |
Chain | Residue | Details |
E | ASP102 | |
E | SER195 | |
E | GLY193 | |
E | HIS57 | |
E | SER214 | |
site_id | MCSA1 |
Number of Residues | 5 |
Details | M-CSA 608 |
Chain | Residue | Details |
E | HIS57 | proton acceptor, proton donor |
E | ASP102 | electrostatic stabiliser |
E | GLY193 | electrostatic stabiliser |
E | SER195 | nucleofuge, nucleophile, proton acceptor, proton donor |
E | SER214 | electrostatic stabiliser |