Functional Information from GO Data
Chain | GOid | namespace | contents |
H | 0004252 | molecular_function | serine-type endopeptidase activity |
H | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SO4 H1259 |
Chain | Residue |
H | MET164 |
H | THR165 |
H | ARG230 |
H | HOH2401 |
H | HOH2402 |
H | HOH2403 |
H | HOH2404 |
H | HOH2405 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CA H1260 |
Chain | Residue |
H | ASP72 |
H | GLU75 |
H | GLU80 |
H | GLU70 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE 346 H1258 |
Chain | Residue |
H | HIS57 |
H | THR98 |
H | THR99 |
H | ASP102 |
H | ASP189 |
H | SER190 |
H | LYS192 |
H | SER195 |
H | SER214 |
H | TRP215 |
H | GLY216 |
H | GLN217 |
H | GLY219 |
H | HOH2340 |
H | HOH2348 |
H | HOH2395 |
H | HOH2398 |
Functional Information from PROSITE/UniProt
site_id | PS00134 |
Number of Residues | 6 |
Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VSAAHC |
Chain | Residue | Details |
H | VAL53-CYS58 | |
site_id | PS00135 |
Number of Residues | 12 |
Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DSckGDSGGPHA |
Chain | Residue | Details |
H | ASP189-ALA200 | |
site_id | PS01186 |
Number of Residues | 16 |
Details | EGF_2 EGF-like domain signature 2. CrCheGYslladgvsC |
Chain | Residue | Details |
L | CYS112-CYS127 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 239 |
Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19167329","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"3264725","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 | HIS57 | |
H | GLY196 | |
site_id | CSA6 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1a0j |
Chain | Residue | Details |
H | ASP102 | |
H | SER195 | |
H | GLY193 | |
H | HIS57 | |