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1SR5

ANTITHROMBIN-ANHYDROTHROMBIN-HEPARIN TERNARY COMPLEX STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0002020molecular_functionprotease binding
A0004867molecular_functionserine-type endopeptidase inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005788cellular_componentendoplasmic reticulum lumen
A0005886cellular_componentplasma membrane
A0007596biological_processblood coagulation
A0007599biological_processhemostasis
A0008201molecular_functionheparin binding
A0030193biological_processregulation of blood coagulation
A0030414molecular_functionpeptidase inhibitor activity
A0031012cellular_componentextracellular matrix
A0042802molecular_functionidentical protein binding
A0070062cellular_componentextracellular exosome
A0072562cellular_componentblood microparticle
B0004252molecular_functionserine-type endopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0007596biological_processblood coagulation
C0004252molecular_functionserine-type endopeptidase activity
C0005509molecular_functioncalcium ion binding
C0006508biological_processproteolysis
C0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
CLEU53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAceGDSGGPFV
ChainResidueDetails
CASP189-VAL200

site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FKANRPFLVfI
ChainResidueDetails
APHE402-ILE412

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Reactive bond","evidences":[{"source":"PubMed","id":"7238875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsGlycosylation: {"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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsGlycosylation: {"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."]}}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"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"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CHIS57

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CSER195
CGLY196

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CSER195
CGLY193

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CGLY193
CHIS57

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
CASP102
CSER195
CHIS57
CGLY196

243531

PDB entries from 2025-10-22

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