Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PG4 B 401 |
Chain | Residue |
A | LEU36 |
A | GLY37 |
B | ARG292 |
B | HOH520 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GSH A 301 |
Chain | Residue |
A | ILE207 |
A | HOH463 |
A | HOH469 |
A | TRP29 |
A | ARG119 |
A | PRO120 |
A | CYS122 |
A | ARG206 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
Chain | Residue | Details |
A | VAL53-CYS58 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLS |
Chain | Residue | Details |
A | ASP189-SER200 | |
site_id | PS00280 |
Number of Residues | 19 |
Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGClgnknnYlreeeC |
Chain | Residue | Details |
B | PHE278-CYS296 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | SITE: Reactive bond => ECO:0000250 |
Chain | Residue | Details |
B | ARG260 | |
A | ASP102 | |
A | SER195 | |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | GLN164 | |