3KCG
Crystal structure of the antithrombin-factor IXa-pentasaccharide complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| H | 0004252 | molecular_function | serine-type endopeptidase activity |
| H | 0006508 | biological_process | proteolysis |
| I | 0002020 | molecular_function | protease binding |
| I | 0004867 | molecular_function | serine-type endopeptidase inhibitor activity |
| I | 0005515 | molecular_function | protein binding |
| I | 0005576 | cellular_component | extracellular region |
| I | 0005615 | cellular_component | extracellular space |
| I | 0005788 | cellular_component | endoplasmic reticulum lumen |
| I | 0005886 | cellular_component | plasma membrane |
| I | 0007596 | biological_process | blood coagulation |
| I | 0007599 | biological_process | hemostasis |
| I | 0008201 | molecular_function | heparin binding |
| I | 0030193 | biological_process | regulation of blood coagulation |
| I | 0030414 | molecular_function | peptidase inhibitor activity |
| I | 0031012 | cellular_component | extracellular matrix |
| I | 0042802 | molecular_function | identical protein binding |
| I | 0070062 | cellular_component | extracellular exosome |
| I | 0072562 | cellular_component | blood microparticle |
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 |
| H | VAL53-CYS58 |
| site_id | PS00284 |
| Number of Residues | 11 |
| Details | SERPIN Serpins signature. FKANRPFLVfI |
| Chain | Residue | Details |
| I | PHE402-ILE412 |
| site_id | PS01186 |
| Number of Residues | 16 |
| Details | EGF_2 EGF-like domain signature 2. CsCteGYrlaenqksC |
| Chain | Residue | Details |
| L | CYS109-CYS124 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 41 |
| Details | Domain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 232 |
| Details | Domain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"20004170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"659613","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"659613","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10467148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20004170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20080729","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1RFN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KCG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LC3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LC5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10467148","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20004170","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20080729","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121197","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20121198","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WPH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WPM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3KCG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LC3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LC5","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Site: {"description":"Reactive bond","evidences":[{"source":"PubMed","id":"7238875","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| 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_FI10 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"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_FI11 |
| Number of Residues | 1 |
| 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_FI12 |
| Number of Residues | 1 |
| 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 |
