Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0005509 | molecular_function | calcium ion binding |
| B | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE GSQ A1244 |
| Chain | Residue |
| A | LYS96 |
| A | GLY216 |
| A | GLY219 |
| A | CYS220 |
| A | GLY226 |
| A | ILE227 |
| A | TYR228 |
| A | HOH2139 |
| A | GLU97 |
| A | THR98 |
| A | TYR99 |
| A | ASP189 |
| A | ALA190 |
| A | GLN192 |
| A | VAL213 |
| A | TRP215 |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC |
| Chain | Residue | Details |
| B | CYS-27-CYS-16 | |
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW |
| Chain | Residue | Details |
| B | GLU-72-TRP-47 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CtCleGfeGKnC |
| Chain | Residue | Details |
| B | CYS-18-CYS-7 | |
| 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. DAcqGDSGGPHV |
| Chain | Residue | Details |
| A | ASP189-VAL200 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CtCleGFegkn....C |
| Chain | Residue | Details |
| B | CYS-18-CYS-7 | |
| B | CYS21-CYS36 | |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
| Chain | Residue | Details |
| B | ASP-42-CYS-18 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | GLU-82 | |
| B | GLU-56 | |
| B | GLU-49 | |
| B | GLU-81 | |
| B | GLU-74 | |
| B | GLU-72 | |
| B | GLU-69 | |
| B | GLU-68 | |
| B | GLU-63 | |
| B | GLU-62 | |
| B | GLU-59 | |
| Chain | Residue | Details |
| B | ASP-25 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | HIS57 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY196 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY193 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 | |
| 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 |
| A | SER195 | |
| A | ASP100 | |
| A | GLY193 | |
| A | 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 | |
