4E06
Anophelin from the malaria vector inhibits thrombin through a novel reverse-binding mechanism
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0005509 | molecular_function | calcium ion binding |
| H | 0006508 | biological_process | proteolysis |
| H | 0007596 | biological_process | blood coagulation |
| I | 0005576 | cellular_component | extracellular region |
| I | 0035821 | biological_process | modulation of process of another organism |
| I | 0090729 | molecular_function | toxin activity |
| I | 0140678 | molecular_function | molecular function inhibitor activity |
| L | 0004252 | molecular_function | serine-type endopeptidase activity |
| L | 0005576 | cellular_component | extracellular region |
| L | 0006508 | biological_process | proteolysis |
| L | 0007596 | biological_process | blood coagulation |
Functional Information from PROSITE/UniProt
| site_id | PS00134 |
| Number of Residues | 6 |
| Details | TRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC |
| Chain | Residue | Details |
| H | LEU359-CYS364 |
| site_id | PS00135 |
| Number of Residues | 12 |
| Details | TRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV |
| Chain | Residue | Details |
| H | ASP519-VAL530 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 22 |
| Details | Region: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Charge relay system"} |
| Chain | Residue | Details |
| 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"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"873923","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Region: {"description":"Blocks exosite I of host thrombin","evidences":[{"source":"PubMed","id":"23223529","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E05","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4E06","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 19 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | Region: {"description":"Blocks active site cleft of host thrombin in a reverse direction compared to substrates","evidences":[{"source":"PubMed","id":"23223529","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4E05","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4E06","evidenceCode":"ECO:0000312"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 10 |
| Details | Compositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
