Functional Information from GO Data
| Chain | GOid | namespace | contents |
| E | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| E | 0005515 | molecular_function | protein binding |
| E | 0006952 | biological_process | defense response |
| E | 0030288 | cellular_component | outer membrane-bounded periplasmic space |
| E | 0042597 | cellular_component | periplasmic space |
| E | 0042803 | molecular_function | protein homodimerization activity |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 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 | 3 |
| Details | BINDING SITE FOR RESIDUE MG L 139 |
| Chain | Residue |
| E | GLN5 |
| L | CGU16 |
| L | CGU26 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG L 140 |
| Chain | Residue |
| L | CGU14 |
| L | CGU19 |
| L | HOH148 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG L 141 |
| Chain | Residue |
| L | CGU25 |
| L | CGU29 |
| L | HOH144 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG H 265 |
| Chain | Residue |
| H | ASP70 |
| H | ASN72 |
| H | GLN75 |
| H | GLU76 |
| H | GLU80 |
| H | HOH273 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA H 266 |
| Chain | Residue |
| H | TYR185 |
| H | ASP185 |
| H | ARG222 |
| H | LYS224 |
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 |
| L | CYS61-CYS72 | |
| site_id | PS00011 |
| Number of Residues | 26 |
| Details | GLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW |
| Chain | Residue | Details |
| L | CGU16-TRP41 | |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CtCleGfeGKnC |
| Chain | Residue | Details |
| L | CYS70-CYS81 | |
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| H | LEU53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV |
| Chain | Residue | Details |
| H | ASP189-VAL200 | |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CtCleGFegkn....C |
| Chain | Residue | Details |
| L | CYS70-CYS81 | |
| L | CYS109-CYS124 | |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC |
| Chain | Residue | Details |
| L | ASP46-CYS70 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 36 |
| Details | Domain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| 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 | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond","evidences":[{"source":"PubMed","id":"35483450","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | HIS57 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | SER195 | |
| H | GLY196 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | SER195 | |
| H | GLY193 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | SER195 | |
| H | HIS57 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | SER195 | |
| H | GLY193 | |
| H | HIS57 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | SER195 | |
| H | ASP100 | |
| H | GLY193 | |
| H | HIS57 | |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| H | ASP102 | |
| H | SER195 | |
| H | HIS57 | |
| H | GLY196 | |
1P0S
