Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 600 |
| Chain | Residue |
| A | HOH16 |
| B | LYS36 |
| B | SER92 |
| B | HOH627 |
| C | TRP237 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 601 |
| Chain | Residue |
| B | HIS40 |
| B | GLU70 |
| B | GLN73 |
| B | LYS82 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR CHAIN D OF TETRAPEPTIDE ADDUCT |
| Chain | Residue |
| C | LYS175 |
| C | SER190 |
| C | MET192 |
| C | GLY193 |
| C | ASP194 |
| C | SER195 |
| C | SER214 |
| C | TRP215 |
| C | GLY216 |
| C | SER217 |
| C | HOH280 |
| D | HOH505 |
| D | HOH506 |
| site_id | BND |
| Number of Residues | 9 |
| Details | SUBSTRATE BINDING SITE |
| Chain | Residue |
| C | SER218 |
| C | CYS220 |
| C | TYR228 |
| C | SER190 |
| C | CYS191 |
| C | MET192 |
| C | VAL213 |
| C | SER214 |
| C | TRP215 |
| site_id | CAT |
| Number of Residues | 3 |
| Details | CATALYTIC CENTER OF THE MOLECULE |
| Chain | Residue |
| B | HIS57 |
| B | ASP102 |
| C | SER195 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
| Chain | Residue | Details |
| B | VAL53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. SScmGDSGGPLV |
| Chain | Residue | Details |
| C | SER189-VAL200 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hja |
| Chain | Residue | Details |
| A | NAL * |
| A | NAL * |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hja |
| Chain | Residue | Details |
| A | NAL * |
| A | NAL * |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hja |
| Chain | Residue | Details |
| A | NAL * |
| A | NAL * |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hja |
| Chain | Residue | Details |
| B | ASP102 | |
| B | HIS57 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hja |
| Chain | Residue | Details |
| C | SER195 | |
| C | GLY193 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1hja |
| Chain | Residue | Details |
| C | SER195 | |
| C | GLY196 | |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 387 |
| Chain | Residue | Details |
| C | GLY193 | electrostatic stabiliser |
| C | SER195 | covalent catalysis |
| C | GLY196 | electrostatic stabiliser |
