1P8J
CRYSTAL STRUCTURE OF THE PROPROTEIN CONVERTASE FURIN
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004252 | molecular_function | serine-type endopeptidase activity |
| A | 0006508 | biological_process | proteolysis |
| A | 0008236 | molecular_function | serine-type peptidase activity |
| B | 0004252 | molecular_function | serine-type endopeptidase activity |
| B | 0006508 | biological_process | proteolysis |
| B | 0008236 | molecular_function | serine-type peptidase activity |
| C | 0004252 | molecular_function | serine-type endopeptidase activity |
| C | 0006508 | biological_process | proteolysis |
| C | 0008236 | molecular_function | serine-type peptidase activity |
| D | 0004252 | molecular_function | serine-type endopeptidase activity |
| D | 0006508 | biological_process | proteolysis |
| D | 0008236 | molecular_function | serine-type peptidase activity |
| E | 0004252 | molecular_function | serine-type endopeptidase activity |
| E | 0006508 | biological_process | proteolysis |
| E | 0008236 | molecular_function | serine-type peptidase activity |
| F | 0004252 | molecular_function | serine-type endopeptidase activity |
| F | 0006508 | biological_process | proteolysis |
| F | 0008236 | molecular_function | serine-type peptidase activity |
| G | 0004252 | molecular_function | serine-type endopeptidase activity |
| G | 0006508 | biological_process | proteolysis |
| G | 0008236 | molecular_function | serine-type peptidase activity |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| H | 0008236 | molecular_function | serine-type peptidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00136 |
| Number of Residues | 12 |
| Details | SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH |
| Chain | Residue | Details |
| A | VAL149-HIS160 |
| site_id | PS00137 |
| Number of Residues | 11 |
| Details | SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA |
| Chain | Residue | Details |
| A | HIS194-ALA204 |
| site_id | PS00138 |
| Number of Residues | 11 |
| Details | SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG |
| Chain | Residue | Details |
| A | GLY366-GLY376 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2512 |
| Details | Domain: {"description":"Peptidase S8","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 264 |
| Details | Domain: {"description":"P/Homo B","evidences":[{"source":"PROSITE-ProRule","id":"PRU01173","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 176 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | Motif: {"description":"Cell attachment site","evidences":[{"source":"PROSITE-ProRule","id":"PRU00293","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 24 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PROSITE-ProRule","id":"PRU01240","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 72 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12794637","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P8J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 120 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12794637","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1P8J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P09958","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 16 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"12794637","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1P8J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| A | SER368 | |
| A | HIS194 | |
| A | ASP153 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| B | SER368 | |
| B | HIS194 | |
| B | ASP153 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| C | SER368 | |
| C | HIS194 | |
| C | ASP153 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| D | SER368 | |
| D | HIS194 | |
| D | ASP153 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| E | SER368 | |
| E | HIS194 | |
| E | ASP153 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| F | SER368 | |
| F | HIS194 | |
| F | ASP153 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| G | SER368 | |
| G | HIS194 | |
| G | ASP153 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1sca |
| Chain | Residue | Details |
| H | SER368 | |
| H | HIS194 | |
| H | ASP153 |
