Functional Information from GO Data
Chain | GOid | namespace | contents |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
L | 0005509 | molecular_function | calcium ion binding |
L | 0005576 | cellular_component | extracellular region |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 187 C 298 |
Chain | Residue |
C | ASN97 |
C | ILE213 |
C | SER214 |
C | TRP215 |
C | GLY216 |
C | GLU217 |
C | GLU219 |
C | CYS220 |
C | GLY226 |
C | TYR99 |
C | ARG143 |
C | PHE174 |
C | ASP189 |
C | SER190 |
C | CYS191 |
C | GLN192 |
C | SER195 |
Functional Information from PROSITE/UniProt
site_id | PS00010 |
Number of Residues | 12 |
Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC |
Chain | Residue | Details |
L | CYS62-CYS73 | |
site_id | PS00011 |
Number of Residues | 26 |
Details | GLA_1 Vitamin K-dependent carboxylation domain. EciEEkCsfeearEvfentektne.FW |
Chain | Residue | Details |
L | GLU17-TRP42 | |
site_id | PS00022 |
Number of Residues | 12 |
Details | EGF_1 EGF-like domain signature 1. CwCqvGfeGKnC |
Chain | Residue | Details |
L | CYS71-CYS82 | |
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
Chain | Residue | Details |
C | VAL53-CYS58 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV |
Chain | Residue | Details |
C | ASP189-VAL200 | |
site_id | PS01186 |
Number of Residues | 12 |
Details | EGF_2 EGF-like domain signature 2. CwCqvGFegkn....C |
Chain | Residue | Details |
L | CYS71-CYS82 | |
L | CYS109-CYS124 | |
site_id | PS01187 |
Number of Residues | 25 |
Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCepnp..........Clnggl..CkDdinsYeC |
Chain | Residue | Details |
L | ASP47-CYS71 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
L | SER3 | |
L | GLY4 | |
L | GLU7 | |
L | ASN13 | |
L | GLU17 | |
Chain | Residue | Details |
L | SER24 | |
C | ILE213 | |
L | PHE25 | |
L | GLU27 | |
L | PHE41 | |
L | TRP42 | |
C | VAL203 | |
C | GLY205 | |
C | PHE208 | |
C | THR210 | |
Chain | Residue | Details |
L | SER123 | |
C | ARG150 | |
Chain | Residue | Details |
L | SER3 | |
L | GLY4 | |
L | GLU7 | |
L | VAL10 | |
L | ASN13 | |
L | GLU17 | |
Chain | Residue | Details |
L | PHE41 | |
C | THR129 | |
Chain | Residue | Details |
L | TYR45 | |
L | SER136 | |
Chain | Residue | Details |
L | GLY133 | |
Chain | Residue | Details |
L | VAL137 | |
Chain | Residue | Details |
L | VAL137 | |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
C | TRP141 | |
C | TYR228 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
C | ASP102 | |
C | HIS57 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
C | SER195 | |
C | GLY196 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
C | SER195 | |
C | GLY193 | |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
C | ASP102 | |
C | SER195 | |
C | 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 |
C | ASP102 | |
C | SER195 | |
C | GLY193 | |
C | HIS57 | |