Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005509 | molecular_function | calcium ion binding |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| C | 0005509 | molecular_function | calcium ion binding |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 7 |
| Chain | Residue |
| A | GOL21 |
| A | PRO166 |
| A | GLY168 |
| A | HOH321 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 21 |
| Chain | Residue |
| A | GLN175 |
| A | LEU177 |
| A | GOL7 |
| A | HOH28 |
| A | PRO169 |
| A | PRO171 |
| A | LYS174 |
| site_id | AC3 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE YET B 1 |
| Chain | Residue |
| B | THR98 |
| B | TYR99 |
| B | GLU147 |
| B | PHE174 |
| B | ALA190 |
| B | SER195 |
| B | VAL213 |
| B | TRP215 |
| B | GLY216 |
| B | GLY218 |
| B | CYS220 |
| B | GLY226 |
| B | ILE227 |
| B | TYR228 |
| B | HOH275 |
| B | HOH302 |
| B | HOH309 |
| B | HOH469 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA B 249 |
| Chain | Residue |
| B | ASP70 |
| B | ASN72 |
| B | GLN75 |
| B | GLU80 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 3 |
| Chain | Residue |
| B | TYR185 |
| B | ASP185 |
| B | ARG222 |
| B | LYS224 |
| B | HOH317 |
| B | HOH323 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 8 |
| Chain | Residue |
| A | PHE139 |
| B | LEU123 |
| B | PRO124 |
| B | ASP239 |
| B | HOH356 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES B 9 |
| Chain | Residue |
| B | PHE101 |
| B | ARG125 |
| B | ASN179 |
| B | ALA233 |
| B | LYS236 |
| B | HOH283 |
| B | HOH299 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 11 |
| Chain | Residue |
| B | TYR185 |
| B | ASP185 |
| B | THR185 |
| B | LYS186 |
| B | HOH442 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACT B 14 |
| Chain | Residue |
| B | GLN133 |
| B | LYS204 |
| B | HOH337 |
| B | HOH373 |
| B | HOH420 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT B 250 |
| Chain | Residue |
| B | PHE50 |
| B | ARG107 |
| B | HOH395 |
| B | HOH551 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS B 251 |
| Chain | Residue |
| B | GLN20 |
| B | MET157 |
| B | LEU158 |
| B | GLU159 |
| B | HOH326 |
| B | HOH346 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE ACT B 252 |
| Chain | Residue |
| B | PHE64 |
| C | SER130 |
| site_id | BC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE YET D 2 |
| Chain | Residue |
| A | ASN120 |
| D | THR98 |
| D | TYR99 |
| D | GLU147 |
| D | ALA190 |
| D | GLN192 |
| D | SER195 |
| D | VAL213 |
| D | TRP215 |
| D | GLY216 |
| D | GLY218 |
| D | CYS220 |
| D | GLY226 |
| D | ILE227 |
| D | TYR228 |
| D | HOH261 |
| D | HOH268 |
| D | HOH295 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 249 |
| Chain | Residue |
| D | ASP70 |
| D | ASN72 |
| D | GLN75 |
| D | GLU80 |
| D | HOH360 |
| D | HOH491 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 4 |
| Chain | Residue |
| D | ARG222 |
| D | LYS224 |
| D | HOH330 |
| D | HOH342 |
| D | TYR185 |
| D | ASP185 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 5 |
| Chain | Residue |
| C | PHE139 |
| D | LEU123 |
| D | PRO124 |
| D | LEU235 |
| D | ASP239 |
| D | HOH340 |
| D | HOH386 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL D 6 |
| Chain | Residue |
| D | ARG93 |
| D | THR95 |
| D | ASP100 |
| D | HOH337 |
| D | HOH367 |
| site_id | BC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES D 10 |
| Chain | Residue |
| D | PHE101 |
| D | ARG125 |
| D | ASN179 |
| D | ALA233 |
| D | LYS236 |
| D | HOH289 |
| D | HOH413 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 12 |
| Chain | Residue |
| D | ARG202 |
| D | LYS204 |
| D | HOH516 |
| site_id | CC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT D 13 |
| Chain | Residue |
| D | ASP185 |
| D | THR185 |
| D | LYS186 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 15 |
| Chain | Residue |
| D | PHE50 |
| D | ARG107 |
| D | HOH402 |
| D | HOH544 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS D 250 |
| Chain | Residue |
| D | GLN20 |
| D | MET157 |
| D | GLU159 |
| D | HOH346 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE ACT D 251 |
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 | CYS101-CYS112 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CtCleGfeGKnC |
| Chain | Residue | Details |
| A | CYS110-CYS121 | |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| B | LEU53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV |
| Chain | Residue | Details |
| B | ASP189-VAL200 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CtCleGFegkn....C |
| Chain | Residue | Details |
| A | CYS110-CYS121 | |
| A | CYS149-CYS164 | |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
| Chain | Residue | Details |
| A | ASP86-CYS110 | |
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 | 232 |
| 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 |
| B | ASP102 | |
| B | SER195 | |
| B | HIS57 | |
| site_id | CSA10 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | SER195 | |
| D | ASP100 | |
| D | GLY193 | |
| D | HIS57 | |
| site_id | CSA11 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | HIS57 | |
| B | GLY196 | |
| site_id | CSA12 |
| 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 | CSA13 |
| 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 | CSA14 |
| 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 | 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 | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | HIS57 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | ASP102 | |
| D | HIS57 | |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | SER195 | |
| B | GLY193 | |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | SER195 | |
| D | GLY193 | |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | SER195 | |
| B | GLY196 | |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| D | SER195 | |
| D | GLY196 | |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | SER195 | |
| B | ASP100 | |
| B | GLY193 | |
| B | HIS57 | |
