Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| B | 0005509 | molecular_function | calcium ion binding |
| 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 | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 501 |
| Chain | Residue |
| A | GLN49 |
| A | BHD63 |
| A | GLY64 |
| A | LEU65 |
| A | GLY66 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 502 |
| Chain | Residue |
| D | GLU80 |
| D | ASP70 |
| D | ASN72 |
| D | GLN75 |
| D | GLU77 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA C 503 |
| Chain | Residue |
| C | ASP70 |
| C | ASN72 |
| C | GLN75 |
| C | GLU76 |
| C | GLU77 |
| C | GLU80 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 4PP C 998 |
| Chain | Residue |
| C | GLU97 |
| C | THR98 |
| C | TYR99 |
| C | PHE174 |
| C | ASP189 |
| C | ALA190 |
| C | CYS191 |
| C | GLN192 |
| C | SER195 |
| C | VAL213 |
| C | GLY216 |
| C | GLY218 |
| C | GLY226 |
| C | HOH558 |
| C | HOH561 |
| C | HOH790 |
| C | HOH794 |
| site_id | AC5 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE 4PP D 999 |
| Chain | Residue |
| D | GLU97 |
| D | THR98 |
| D | TYR99 |
| D | PHE174 |
| D | ASP189 |
| D | ALA190 |
| D | CYS191 |
| D | GLN192 |
| D | SER195 |
| D | VAL213 |
| D | TRP215 |
| D | GLY216 |
| D | GLY218 |
| D | GLY226 |
| D | HOH647 |
| D | HOH650 |
| D | HOH670 |
| D | HOH672 |
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 |
| A | CYS61-CYS72 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CtCleGfeGKnC |
| Chain | Residue | Details |
| A | CYS70-CYS81 | |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| C | LEU53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV |
| Chain | Residue | Details |
| C | ASP189-VAL200 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CtCleGFegkn....C |
| Chain | Residue | Details |
| A | CYS70-CYS81 | |
| A | CYS109-CYS124 | |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
| Chain | Residue | Details |
| A | ASP46-CYS70 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 80 |
| Details | Domain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 464 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system"} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | ASP102 | |
| C | SER195 | |
| C | HIS57 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | HIS57 | |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | ASP102 | |
| C | SER195 | |
| C | GLY193 | |
| C | HIS57 | |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | GLY193 | |
| D | HIS57 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | ASP102 | |
| C | SER195 | |
| C | HIS57 | |
| C | GLY196 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | SER195 | |
| D | HIS57 | |
| D | GLY196 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| C | SER195 | |
| C | ASP100 | |
| C | GLY193 | |
| C | HIS57 | |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | SER195 | |
| D | ASP100 | |
| D | GLY193 | |
| D | HIS57 | |
1XKB
