Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
I | 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 PO4 I 304 |
Chain | Residue |
A | HIS451 |
I | ARG265 |
I | TYR280 |
I | HOH327 |
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 | VAL443-CYS448 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPLA |
Chain | Residue | Details |
A | ASP592-ALA603 | |
site_id | PS00280 |
Number of Residues | 19 |
Details | BPTI_KUNITZ_1 Pancreatic trypsin inhibitor (Kunitz) family signature. FvyGGClgnknnYlreeeC |
Chain | Residue | Details |
I | 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 |
I | ARG260 | |
A | ASP497 | |
A | SER598 | |
Chain | Residue | Details |
A | ASN468 | |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN546 | |