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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 999 |
| Chain | Residue |
| A | ASP71 |
| A | ASN73 |
| A | GLN76 |
| A | GLU77 |
| A | GLU81 |
| A | HOH361 |
| A | HOH385 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE T87 A 1 |
| Chain | Residue |
| A | THR99 |
| A | TYR100 |
| A | PHE177 |
| A | ASP194 |
| A | ALA195 |
| A | GLN197 |
| A | SER200 |
| A | SER219 |
| A | TRP220 |
| A | GLY221 |
| A | GLY223 |
| A | GLY231 |
| A | HOH309 |
| A | HIS57 |
| A | GLU98 |
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 | CYS227-CYS238 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CtCleGfeGKnC |
| Chain | Residue | Details |
| B | CYS236-CYS247 | |
| 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 | ASP194-VAL205 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CtCleGFegkn....C |
| Chain | Residue | Details |
| B | CYS236-CYS247 | |
| B | CYS275-CYS290 | |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
| Chain | Residue | Details |
| B | ASP212-CYS236 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 232 |
| 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"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Domain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP103 | |
| A | HIS57 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | GLY201 | |
| A | SER200 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | GLY198 | |
| A | SER200 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP103 | |
| A | SER200 | |
| A | HIS57 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | GLY198 | |
| A | SER200 | |
| A | HIS57 | |
| A | ASP101 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP103 | |
| A | GLY201 | |
| A | SER200 | |
| A | HIS57 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP103 | |
| A | GLY198 | |
| A | SER200 | |
| A | HIS57 | |
