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 | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 6 |
| Chain | Residue |
| A | VAL148 |
| A | CYS149 |
| A | LEU157 |
| A | HOH198 |
| A | HOH406 |
| A | HOH598 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 7 |
| Chain | Residue |
| A | TYR155 |
| A | THR156 |
| A | LEU157 |
| A | HOH406 |
| A | GOL9 |
| A | SER150 |
| A | CYS151 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 9 |
| Chain | Residue |
| A | GOL7 |
| A | GLY154 |
| A | TYR155 |
| A | THR156 |
| A | THR167 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MBM B 1 |
| Chain | Residue |
| B | THR98 |
| B | TYR99 |
| B | GLU147 |
| B | PHE174 |
| B | ALA190 |
| B | GLN192 |
| B | SER195 |
| B | VAL213 |
| B | TRP215 |
| B | GLY216 |
| B | GLY218 |
| B | CYS220 |
| B | GLY226 |
| B | ILE227 |
| B | TYR228 |
| B | HOH262 |
| B | HOH273 |
| B | HOH287 |
| B | HOH454 |
| C | GLN96 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 249 |
| Chain | Residue |
| B | ASP70 |
| B | ASN72 |
| B | GLN75 |
| B | GLU80 |
| B | HOH567 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 3 |
| Chain | Residue |
| B | TYR185 |
| B | ASP185 |
| B | ARG222 |
| B | LYS224 |
| B | HOH304 |
| B | HOH504 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 8 |
| Chain | Residue |
| B | LEU123 |
| B | PRO124 |
| B | HOH252 |
| B | HOH379 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 14 |
| Chain | Residue |
| B | THR132 |
| D | VAL88 |
| D | ILE89 |
| D | HOH647 |
| site_id | AC9 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MBM D 2 |
| Chain | Residue |
| A | THR92 |
| A | SER93 |
| A | GLN96 |
| A | ASN120 |
| D | HOH11 |
| D | THR98 |
| D | TYR99 |
| D | GLU147 |
| D | ALA190 |
| D | GLN192 |
| D | VAL213 |
| D | TRP215 |
| D | GLY216 |
| D | GLY218 |
| D | CYS220 |
| D | GLY226 |
| D | ILE227 |
| D | TYR228 |
| D | HOH260 |
| D | HOH282 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA D 249 |
| Chain | Residue |
| D | ASP70 |
| D | ASN72 |
| D | GLN75 |
| D | GLU80 |
| D | HOH662 |
| D | HOH882 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA D 4 |
| Chain | Residue |
| D | TYR185 |
| D | ASP185 |
| D | ARG222 |
| D | LYS224 |
| D | HOH271 |
| D | HOH399 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL D 5 |
| Chain | Residue |
| C | HOH620 |
| D | PRO124 |
| D | HOH268 |
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 | 6 |
| Details | ACT_SITE: Charge relay system |
| Chain | Residue | Details |
| B | HIS57 | |
| B | ASP102 | |
| B | SER195 | |
| D | HIS57 | |
| D | ASP102 | |
| D | SER195 | |
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 | |
