Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | binding site for residue CA A 301 |
| Chain | Residue |
| A | ASN146 |
| A | ASP147 |
| A | 0GJ302 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue 0GJ A 302 |
| Chain | Residue |
| A | GLY193 |
| A | SER195 |
| A | SER214 |
| A | TRP215 |
| A | GLY216 |
| A | GLY219 |
| A | GLY226 |
| A | CA301 |
| A | HIS57 |
| A | GLN98 |
| A | ASP189 |
| A | SER190 |
| A | CYS191 |
| A | GLN192 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | binding site for residue CA B 301 |
| Chain | Residue |
| B | ASP147 |
| B | 0GJ302 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue 0GJ B 302 |
| Chain | Residue |
| B | HIS57 |
| B | GLN98 |
| B | ASP189 |
| B | SER190 |
| B | CYS191 |
| B | GLN192 |
| B | GLY193 |
| B | SER195 |
| B | SER214 |
| B | TRP215 |
| B | GLY216 |
| B | GLY219 |
| B | GLY226 |
| B | CA301 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue CA D 301 |
| Chain | Residue |
| D | ASN146 |
| D | ASP147 |
| D | 0GJ302 |
| site_id | AC6 |
| Number of Residues | 14 |
| Details | binding site for residue 0GJ D 302 |
| Chain | Residue |
| D | HIS57 |
| D | GLN98 |
| D | ASP189 |
| D | SER190 |
| D | CYS191 |
| D | GLN192 |
| D | GLY193 |
| D | SER195 |
| D | SER214 |
| D | TRP215 |
| D | GLY216 |
| D | GLY219 |
| D | GLY226 |
| D | CA301 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide 0GJ C 301 and HIS C 57 |
| Chain | Residue |
| C | ALA55 |
| C | ALA56 |
| C | CYS58 |
| C | VAL59 |
| C | GLY60 |
| C | PHE94 |
| C | GLN98 |
| C | ASP102 |
| C | ASP189 |
| C | SER190 |
| C | CYS191 |
| C | GLN192 |
| C | GLY193 |
| C | SER195 |
| C | SER214 |
| C | TRP215 |
| C | GLY216 |
| C | GLY219 |
| C | GLY226 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | binding site for Di-peptide 0GJ C 301 and SER C 195 |
| Chain | Residue |
| C | CYS42 |
| C | GLY43 |
| C | HIS57 |
| C | CYS58 |
| C | GLN98 |
| C | ASP189 |
| C | SER190 |
| C | CYS191 |
| C | GLN192 |
| C | GLY193 |
| C | ASP194 |
| C | GLY196 |
| C | GLY197 |
| C | VAL213 |
| C | SER214 |
| C | TRP215 |
| C | GLY216 |
| C | GLY219 |
| C | GLY226 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| A | LEU53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLV |
| Chain | Residue | Details |
| A | ASP189-VAL200 | |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH |
| Chain | Residue | Details |
| E | TYR194-HIS200 | |
| F | TYR192-HIS198 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 964 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Charge relay system"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]} |