1ATH
THE INTACT AND CLEAVED HUMAN ANTITHROMBIN III COMPLEX AS A MODEL FOR SERPIN-PROTEINASE INTERACTIONS
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0002020 | molecular_function | protease binding |
| A | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0007596 | biological_process | blood coagulation |
| A | 0007599 | biological_process | hemostasis |
| A | 0008201 | molecular_function | heparin binding |
| A | 0030193 | biological_process | regulation of blood coagulation |
| A | 0030414 | molecular_function | peptidase inhibitor activity |
| A | 0031012 | cellular_component | extracellular matrix |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0072562 | cellular_component | blood microparticle |
| B | 0002020 | molecular_function | protease binding |
| B | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005576 | cellular_component | extracellular region |
| B | 0005615 | cellular_component | extracellular space |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0007596 | biological_process | blood coagulation |
| B | 0007599 | biological_process | hemostasis |
| B | 0008201 | molecular_function | heparin binding |
| B | 0030193 | biological_process | regulation of blood coagulation |
| B | 0030414 | molecular_function | peptidase inhibitor activity |
| B | 0031012 | cellular_component | extracellular matrix |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0072562 | cellular_component | blood microparticle |
Functional Information from PDB Data
| site_id | P1 |
| Number of Residues | 2 |
| Details | CLEAVAGE SITE BY SERINE PROTEASES LIKE THROMBIN |
| Chain | Residue |
| A | ARG393 |
| B | ARG393 |
Functional Information from PROSITE/UniProt
| site_id | PS00284 |
| Number of Residues | 11 |
| Details | SERPIN Serpins signature. FKANRPFLVfI |
| Chain | Residue | Details |
| A | PHE402-ILE412 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Reactive bond","evidences":[{"source":"PubMed","id":"7238875","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) (complex) asparagine","evidences":[{"source":"PubMed","id":"14760718","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15084671","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19838169","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1979","firstPage":"43","lastPage":"54","publisher":"Elsevier","address":"Amsterdam","bookName":"The physiological inhibitors of blood coagulation and fibrinolysis","title":"Primary structure of antithrombin-III (heparin cofactor). Partial homology between alpha-1-antitrypsin and antithrombin-III.","editors":["Collen D.","Wiman B.","Verstraete M."],"authors":["Petersen T.E.","Dudek-Wojciechowska G.","Sottrup-Jensen L.","Magnusson S."]}}]} |
| Chain | Residue | Details |
