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 | 15 |
| Details | BINDING SITE FOR RESIDUE ENS B 301 |
| Chain | Residue |
| B | GLU97 |
| B | TRP215 |
| B | GLY216 |
| B | GLY218 |
| B | CYS220 |
| B | GLY226 |
| B | ILE227 |
| B | THR98 |
| B | TYR99 |
| B | GLU147 |
| B | ASP189 |
| B | ALA190 |
| B | CYS191 |
| B | GLN192 |
| B | VAL213 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ENS D 301 |
| Chain | Residue |
| A | ASN120 |
| D | GLU97 |
| D | TYR99 |
| D | GLU147 |
| D | ASP189 |
| D | ALA190 |
| D | CYS191 |
| D | GLN192 |
| D | VAL213 |
| D | TRP215 |
| D | GLY216 |
| D | GLY218 |
| D | CYS220 |
| D | GLY226 |
| D | ILE227 |
| D | HOH333 |
| D | HOH374 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 302 |
| Chain | Residue |
| B | ASP70 |
| B | ASN72 |
| B | THR73 |
| B | GLN75 |
| B | GLU80 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA D 302 |
| Chain | Residue |
| D | ASP70 |
| D | ASN72 |
| D | GLN75 |
| D | GLU80 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 303 |
| Chain | Residue |
| B | TYR185 |
| B | ASP185 |
| B | LYS186 |
| B | ALA221 |
| B | ARG222 |
| B | LYS224 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA D 303 |
| Chain | Residue |
| D | TYR185 |
| D | ASP185 |
| D | LYS186 |
| D | ALA221 |
| D | ARG222 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES B 304 |
| Chain | Residue |
| B | ARG125 |
| B | ASN179 |
| B | ALA233 |
| B | LYS236 |
| B | HOH366 |
| B | HOH412 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES D 304 |
| Chain | Residue |
| D | PHE101 |
| D | ARG125 |
| D | ASN179 |
| D | ALA233 |
| D | LYS236 |
| D | HOH349 |
| D | HOH389 |
| D | HOH418 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 201 |
| Chain | Residue |
| A | PRO166 |
| A | GLY168 |
| A | GOL203 |
| A | HOH215 |
| A | HOH222 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | LEU157 |
| A | HOH213 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 203 |
| Chain | Residue |
| A | PRO171 |
| A | LYS174 |
| A | LEU177 |
| A | GOL201 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 305 |
| Chain | Residue |
| B | PRO124 |
| B | LEU235 |
| B | ASP239 |
| B | HOH337 |
| B | HOH398 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 305 |
| Chain | Residue |
| D | LEU123 |
| D | PRO124 |
| D | ASP239 |
| D | HOH412 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL D 306 |
| Chain | Residue |
| D | ARG93 |
| D | THR95 |
| D | ASP100 |
| D | HOH367 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL D 307 |
| Chain | Residue |
| A | SER130 |
| B | THR132 |
| D | VAL87 |
| D | VAL88 |
| D | ILE89 |
| D | HOH378 |
| site_id | BC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ACT B 306 |
| Chain | Residue |
| B | ASP185 |
| B | THR185 |
| B | LYS186 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACT D 308 |
| Chain | Residue |
| D | TYR185 |
| D | ASP185 |
| D | THR185 |
| D | LYS186 |
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 | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
| Chain | Residue | Details |
| A | ASP86-CYS110 | |
| 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 | 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 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| B | HIS57 | |
| B | ASP102 | |
| B | SER195 | |
| D | HIS57 | |
| D | ASP102 | |
| D | SER195 | |
