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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1TB6

2.5A Crystal Structure of the Antithrombin-Thrombin-Heparin Ternary Complex

Functional Information from GO Data
ChainGOidnamespacecontents
H0004252molecular_functionserine-type endopeptidase activity
H0005509molecular_functioncalcium ion binding
H0006508biological_processproteolysis
H0007596biological_processblood coagulation
I0002020molecular_functionprotease binding
I0004867molecular_functionserine-type endopeptidase inhibitor activity
I0005515molecular_functionprotein binding
I0005576cellular_componentextracellular region
I0005615cellular_componentextracellular space
I0005788cellular_componentendoplasmic reticulum lumen
I0005886cellular_componentplasma membrane
I0007596biological_processblood coagulation
I0007599biological_processhemostasis
I0008201molecular_functionheparin binding
I0030193biological_processregulation of blood coagulation
I0030414molecular_functionpeptidase inhibitor activity
I0031012cellular_componentextracellular matrix
I0042802molecular_functionidentical protein binding
I0070062cellular_componentextracellular exosome
I0072562cellular_componentblood microparticle
L0004252molecular_functionserine-type endopeptidase activity
L0005576cellular_componentextracellular region
L0006508biological_processproteolysis
L0007596biological_processblood coagulation
Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. FKANRPFLVfI
ChainResidueDetails
IPHE402-ILE412
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues254
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues22
DetailsRegion: {"description":"High affinity receptor-binding region which is also known as the TP508 peptide"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails
site_idSWS_FT_FI4
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
site_idSWS_FT_FI5
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsSite: {"description":"Reactive bond","evidences":[{"source":"PubMed","id":"7238875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
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_FI8
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_FI9
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_FI10
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
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HHIS57
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HALA195
HGLY196
site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HALA195
HGLY193
site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HALA195
HGLY193
HHIS57
site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1a0j
ChainResidueDetails
HASP102
HALA195
HHIS57

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