1NQ9

Crystal Structure of Antithrombin in the Pentasaccharide-Bound Intermediate State

Functional Information from GO Data

Chain	GOid	namespace	contents
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
L	0002020	molecular_function	protease binding
L	0004867	molecular_function	serine-type endopeptidase inhibitor activity
L	0005515	molecular_function	protein binding
L	0005576	cellular_component	extracellular region
L	0005615	cellular_component	extracellular space
L	0005788	cellular_component	endoplasmic reticulum lumen
L	0005886	cellular_component	plasma membrane
L	0007596	biological_process	blood coagulation
L	0007599	biological_process	hemostasis
L	0008201	molecular_function	heparin binding
L	0030193	biological_process	regulation of blood coagulation
L	0030414	molecular_function	peptidase inhibitor activity
L	0031012	cellular_component	extracellular matrix
L	0042802	molecular_function	identical protein binding
L	0070062	cellular_component	extracellular exosome
L	0072562	cellular_component	blood microparticle

Functional Information from PROSITE/UniProt

site_id	PS00284
Number of Residues	11
Details	SERPIN Serpins signature. FKANRPFLVfI

Chain	Residue	Details
I	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

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---