Functional Information from GO Data
| Chain | GOid | namespace | contents | 
| A | 0004252 | molecular_function | serine-type endopeptidase activity | 
| A | 0005515 | molecular_function | protein binding | 
| 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 | 
| B | 0004252 | molecular_function | serine-type endopeptidase activity | 
| B | 0005515 | molecular_function | protein binding | 
| B | 0005576 | cellular_component | extracellular region | 
| B | 0005615 | cellular_component | extracellular space | 
| B | 0006508 | biological_process | proteolysis | 
| B | 0008233 | molecular_function | peptidase activity | 
| B | 0008236 | molecular_function | serine-type peptidase activity | 
| B | 0016787 | molecular_function | hydrolase activity | 
| B | 0022617 | biological_process | extracellular matrix disassembly | 
| B | 0030141 | cellular_component | secretory granule | 
| B | 0031214 | biological_process | biomineral tissue development | 
| B | 0046872 | molecular_function | metal ion binding | 
| B | 0051604 | biological_process | protein maturation | 
| B | 0097186 | biological_process | amelogenesis | 
Functional Information from PDB Data
| site_id | AC1 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE NA A 401 | 
| Chain | Residue | 
| A | LEU99 | 
| A | ASP102 | 
| A | MET180 | 
| A | SER214 | 
| A | HOH412 | 
| site_id | AC2 | 
| Number of Residues | 5 | 
| Details | BINDING SITE FOR RESIDUE NA A 402 | 
| Chain | Residue | 
| A | CYS232 | 
| A | PRO129 | 
| A | GLN210 | 
| A | ASN230 | 
| A | LEU231 | 
| site_id | AC3 | 
| Number of Residues | 2 | 
| Details | BINDING SITE FOR RESIDUE CL B 403 | 
| Chain | Residue | 
| B | LEU98 | 
| B | SER164 | 
| site_id | AC4 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE CL A 404 | 
| Chain | Residue | 
| A | LEU98 | 
| A | VAL163 | 
| A | SER164 | 
| A | VAL167 | 
| A | HOH498 | 
| A | HOH529 | 
| site_id | AC5 | 
| Number of Residues | 7 | 
| Details | BINDING SITE FOR RESIDUE NI A 405 | 
| Chain | Residue | 
| A | HIS25 | 
| A | GLU77 | 
| A | HOH480 | 
| A | HOH483 | 
| A | HOH486 | 
| A | HOH557 | 
| A | HOH563 | 
| site_id | AC6 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE NI B 406 | 
| Chain | Residue | 
| B | HIS25 | 
| B | GLU77 | 
| B | HOH534 | 
| B | HOH535 | 
| B | HOH536 | 
| B | HOH537 | 
| site_id | AC7 | 
| Number of Residues | 4 | 
| Details | BINDING SITE FOR RESIDUE NI B 407 | 
| Chain | Residue | 
| B | THR64 | 
| B | HOH538 | 
| B | HOH539 | 
| B | HOH540 | 
| site_id | AC8 | 
| Number of Residues | 6 | 
| Details | BINDING SITE FOR RESIDUE NI A 408 | 
| Chain | Residue | 
| A | ASN37 | 
| A | HOH531 | 
| A | HOH550 | 
| A | HOH556 | 
| A | HOH558 | 
| A | HOH560 | 
| site_id | AC9 | 
| Number of Residues | 9 | 
| Details | BINDING SITE FOR RESIDUE PBZ A 301 | 
| Chain | Residue | 
| A | ASP189 | 
| A | SER190 | 
| A | ASN192 | 
| A | SER195 | 
| A | VAL213 | 
| A | PHE215 | 
| A | CYS220 | 
| A | GLY226 | 
| A | HOH424 | 
| site_id | BC1 | 
| Number of Residues | 10 | 
| Details | BINDING SITE FOR RESIDUE PBZ B 302 | 
| Chain | Residue | 
| B | ASP189 | 
| B | SER190 | 
| B | SER195 | 
| B | VAL213 | 
| B | PHE215 | 
| B | GLY216 | 
| B | LYS217 | 
| B | CYS220 | 
| B | GLY226 | 
| B | HOH415 | 
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 | 442 | 
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} | 
| site_id | SWS_FT_FI2 | 
| Number of Residues | 6 | 
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 4 | 
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16950394","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 2 | 
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| A | ASP102 |  | 
| A | SER195 |  | 
| A | HIS57 |  | 
| site_id | CSA2 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| B | ASP102 |  | 
| B | SER195 |  | 
| B | HIS57 |  | 
| site_id | CSA3 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| A | SER195 |  | 
| A | ALA100 |  | 
| A | HIS57 |  | 
| A | GLY196 |  | 
| site_id | CSA4 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| B | SER195 |  | 
| B | ALA100 |  | 
| B | HIS57 |  | 
| B | GLY196 |  | 
| site_id | CSA5 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| A | ASP102 |  | 
| A | SER195 |  | 
| A | GLY193 |  | 
| A | HIS57 |  | 
| site_id | CSA6 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| B | ASP102 |  | 
| B | SER195 |  | 
| B | GLY193 |  | 
| B | HIS57 |  | 
| site_id | CSA7 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| A | ASP102 |  | 
| A | SER195 |  | 
| A | HIS57 |  | 
| A | GLY196 |  | 
| site_id | CSA8 | 
| Number of Residues | 4 | 
| Details | Annotated By Reference To The Literature 1a0j | 
| Chain | Residue | Details | 
| B | ASP102 |  | 
| B | SER195 |  | 
| B | HIS57 |  | 
| B | GLY196 |  |