Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 1 |
| Chain | Residue |
| B | HIS91 |
| B | LEU233 |
| B | PHE234 |
| B | TRP237 |
| B | HOH381 |
| B | HOH420 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 3 |
| Chain | Residue |
| B | PRO28 |
| B | HIS71 |
| B | MET117 |
| B | HOH448 |
| B | GLY25 |
| B | GLU26 |
| B | TRP27 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 4 |
| Chain | Residue |
| B | PHE184 |
| B | LEU185 |
| B | SER186 |
| B | HOH384 |
| B | HOH508 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 6 |
| Chain | Residue |
| B | ARG230 |
| B | PRO232 |
| B | LEU233 |
| B | HOH367 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO B 7 |
| Chain | Residue |
| B | GLU26 |
| B | TRP29 |
| B | ILE207 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 8 |
| Chain | Residue |
| B | ALA135 |
| B | ARG161 |
| B | HOH496 |
| B | HOH516 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 215 |
| Chain | Residue |
| C | GLN37 |
| C | LYS39 |
| C | LYS42 |
| C | LYS45 |
| C | HOH337 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO C 216 |
| Chain | Residue |
| C | SER65 |
| C | GLY66 |
| C | ASP70 |
| C | PHE71 |
| C | THR72 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 217 |
| Chain | Residue |
| B | GLY18 |
| C | VAL110 |
| C | ALA111 |
| C | ALA112 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 243 |
| Chain | Residue |
| C | TYR96 |
| D | GLN100 |
| D | ASN100 |
| D | VAL100 |
| D | SER100 |
| D | PHE100 |
| D | HOH287 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 2 |
| Chain | Residue |
| A | PHE184 |
| A | LEU185 |
| A | SER186 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 12 |
| Chain | Residue |
| A | PRO178 |
| A | ARG179 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 13 |
| Chain | Residue |
| A | HIS91 |
| A | TYR101 |
| A | PHE234 |
| A | TRP237 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 E 215 |
| Chain | Residue |
| E | GLN37 |
| E | LYS39 |
| E | LYS42 |
| E | LYS45 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO E 216 |
| Chain | Residue |
| E | GLN38 |
| E | GLY41 |
| E | LYS42 |
| F | TYR91 |
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 |
| B | VAL53-CYS58 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPLS |
| Chain | Residue | Details |
| B | ASP189-SER200 | |
| site_id | PS00290 |
| Number of Residues | 7 |
| Details | IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH |
| Chain | Residue | Details |
| D | TYR194-HIS200 | |
| C | TYR192-HIS198 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 478 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Active site: {"description":"Charge relay system"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 194 |
| Details | Domain: {"description":"Ig-like"} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 48 |
| Details | Region: {"description":"Framework-1","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 14 |
| Details | Region: {"description":"Complementarity-determining-1","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 32 |
| Details | Region: {"description":"Framework-2","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 14 |
| Details | Region: {"description":"Complementarity-determining-2","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 74 |
| Details | Region: {"description":"Framework-3","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Region: {"description":"Complementarity-determining-3","evidences":[{"source":"UniProtKB","id":"P23083","evidenceCode":"ECO:0000250"}]} |
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 |
| A | ASP102 | |
| A | SER195 | |
| A | GLY193 | |
| A | 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 |
| A | ASP102 | |
| A | SER195 | |
| A | HIS57 | |
| A | GLY196 | |
| site_id | CSA13 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | SER195 | |
| B | GLY193 | |
| B | HIS57 | |
| B | ASP96 | |
| B | SER214 | |
| site_id | CSA14 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | SER195 | |
| A | GLY193 | |
| A | HIS57 | |
| A | ASP96 | |
| A | SER214 | |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| A | ASP102 | |
| A | SER195 | |
| A | 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 |
| A | ASP102 | |
| A | 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 |
| A | SER195 | |
| A | 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 |
| A | SER195 | |
| A | GLY196 | |
| site_id | CSA9 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | ASP102 | |
| B | SER195 | |
| B | GLY193 | |
| B | HIS57 | |
