Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0022617 | biological_process | extracellular matrix disassembly |
| A | 0030141 | cellular_component | secretory granule |
| A | 0031214 | biological_process | biomineral tissue development |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051604 | biological_process | protein maturation |
| A | 0097186 | biological_process | amelogenesis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR CHAIN B OF TRYPSIN INHIBITOR 1 |
| Chain | Residue |
| A | LEU40 |
| A | ASP189 |
| A | SER190 |
| A | CYS191 |
| A | ASN192 |
| A | GLY193 |
| A | ASP194 |
| A | SER195 |
| A | SER214 |
| A | PHE215 |
| A | GLY216 |
| A | PHE41 |
| A | LYS217 |
| A | ALA218 |
| A | CYS220 |
| A | HOH322 |
| A | HOH348 |
| B | HOH101 |
| B | HOH102 |
| B | HOH103 |
| B | HOH104 |
| B | HOH105 |
| A | CYS42 |
| B | HOH106 |
| B | HOH108 |
| A | HIS57 |
| A | TYR94 |
| A | LEU99 |
| A | MET151 |
| A | TYR172 |
| A | LEU175 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LSAAHC |
| Chain | Residue | Details |
| A | LEU53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScnGDSGGPLI |
| Chain | Residue | Details |
| A | ASP189-ILE200 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 221 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | Peptide: {"description":"Trypsin inhibitor 1","featureId":"PRO_0000042673"} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond","evidences":[{"source":"UniProtKB","id":"P81705","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Cross-link: {"description":"Cyclopeptide (Gly-Asp)"} |
