Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 GOL A 1 |
| Chain | Residue |
| A | GLU313 |
| A | LEU326 |
| A | SER328 |
| A | SER442 |
| B | HOH5 |
| B | LYS457 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 2 |
| Chain | Residue |
| B | HOH12 |
| A | MET342 |
| A | ASP343 |
| A | THR344 |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC |
| Chain | Residue | Details |
| B | VAL486-CYS491 | |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcaGDSGGPMV |
| Chain | Residue | Details |
| B | ASP640-VAL651 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 65 |
| Details | Domain: {"description":"Sushi 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 69 |
| Details | Domain: {"description":"Sushi 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00302","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19139490","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11290788","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 247 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | HIS490 | |
| B | SER646 | |
| B | ASP552 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | HIS490 | |
| B | ASP552 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | GLY644 | |
| B | SER646 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | SER646 | |
| B | GLY647 | |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | GLY644 | |
| B | HIS490 | |
| B | SER646 | |
| B | ASP552 | |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a0j |
| Chain | Residue | Details |
| B | HIS490 | |
| B | SER646 | |
| B | ASP552 | |
| B | GLY647 | |
