1ID5

CRYSTAL STRUCTURE OF BOVINE THROMBIN COMPLEX WITH PROTEASE INHIBITOR ECOTIN

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth L]	d1id5.1	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Thrombin	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B [auth H]	d1id5.1	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Thrombin	(Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
C [auth I]	d1id5i_	All beta proteins	Ecotin, trypsin inhibitor	Ecotin, trypsin inhibitor	Ecotin, trypsin inhibitor	Ecotin, trypsin inhibitor	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C [auth I]	SCOP2B Superfamily	Ecotin trypsin inhibitor	8041127	3001256	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
C [auth I]	Ecotin	e1id5I1	A: beta sandwiches	X: Ecotin, trypsin inhibitor (From Topology)	H: Ecotin, trypsin inhibitor (From Topology)	T: Ecotin, trypsin inhibitor	F: Ecotin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth H]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
C [auth I]	2.60.40.550	Mainly Beta	Sandwich	Immunoglobulin-like	Ecotin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth L]	PF09396	Thrombin light chain (Thrombin_light)	Thrombin light chain	Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleave ...	Thrombin is an enzyme that cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII. Prothrombin is activated on the surface of a phospholipid membrane where factor Xa removes the activation peptide and cleaves the remaining part into light and heavy chains. This domain corresponds to the light chain of thrombin.	Domain
B [auth H]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
C [auth I]	PF03974	Ecotin (Ecotin)	Ecotin	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth L]	THROMBIN	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity protein-containing complex binding fibrinogen binding	cellular component organization cellular component biogenesis protein polymerization cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis multicellular organismal process regulation of body fluid levels wound healing response to stimulus cell activation hemostasis cellular component organization cellular component biogenesis protein polymerization cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis multicellular organismal process regulation of body fluid levels wound healing response to stimulus cell activation hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding platelet activation acute-phase response defense response inflammatory response acute inflammatory response positive regulation of coagulation regulation of response to external stimulus positive regulation of biological process positive regulation of blood coagulation regulation of response to wounding regulation of coagulation positive regulation of response to stimulus regulation of response to stress regulation of multicellular organismal process positive regulation of hemostasis regulation of hemostasis positive regulation of response to wounding regulation of biological process regulation of blood coagulation response to external stimulus positive regulation of wound healing regulation of response to stimulus regulation of wound healing positive regulation of multicellular organismal process organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix cellular anatomical entity extracellular region extracellular space
B [auth H]	THROMBIN	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity cation binding ion binding binding calcium ion binding metal ion binding small molecule binding peptidase activity catalytic activity, acting on a protein serine hydrolase activity serine-type peptidase activity hydrolase activity serine-type endopeptidase activity catalytic activity endopeptidase activity protein-containing complex binding fibrinogen binding	cellular component organization cellular component biogenesis protein polymerization cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis multicellular organismal process regulation of body fluid levels wound healing response to stimulus cell activation hemostasis cellular component organization cellular component biogenesis protein polymerization cellular component assembly protein-containing complex organization protein-containing complex assembly cellular process cellular component organization or biogenesis multicellular organismal process regulation of body fluid levels wound healing response to stimulus cell activation hemostasis biological regulation blood coagulation response to stress coagulation regulation of biological quality response to wounding platelet activation acute-phase response defense response inflammatory response acute inflammatory response positive regulation of coagulation regulation of response to external stimulus positive regulation of biological process positive regulation of blood coagulation regulation of response to wounding regulation of coagulation positive regulation of response to stimulus regulation of response to stress regulation of multicellular organismal process positive regulation of hemostasis regulation of hemostasis positive regulation of response to wounding regulation of biological process regulation of blood coagulation response to external stimulus positive regulation of wound healing regulation of response to stimulus regulation of wound healing positive regulation of multicellular organismal process organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery extracellular matrix external encapsulating structure collagen-containing extracellular matrix cellular anatomical entity extracellular region extracellular space
C [auth I]	ECOTIN	enzyme regulator activity molecular function inhibitor activity peptidase regulator activity serine-type endopeptidase inhibitor activity molecular function regulator activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity	-	outer membrane-bounded periplasmic space cell envelope periplasmic space cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth L]	IPR018992	Thrombin light chain	Domain
A [auth L]	IPR000294	Gamma-carboxyglutamic acid-rich (GLA) domain	Domain
A [auth L]	IPR037111	Thrombin light chain domain superfamily	Homologous Superfamily
A [auth L]	IPR003966	Prothrombin/thrombin	Family
A [auth L]	IPR018056	Kringle, conserved site	Conserved Site
A [auth L]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A [auth L]	IPR013806	Kringle-like fold	Homologous Superfamily
A [auth L]	IPR038178	Kringle superfamily	Homologous Superfamily
A [auth L]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A [auth L]	IPR001314	Peptidase S1A, chymotrypsin family	Family
A [auth L]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
A [auth L]	IPR001254	Serine proteases, trypsin domain	Domain
A [auth L]	IPR035972	Gamma-carboxyglutamic acid-rich (GLA) domain superfamily	Homologous Superfamily
A [auth L]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A [auth L]	IPR000001	Kringle	Domain
B [auth H]	IPR018992	Thrombin light chain	Domain
B [auth H]	IPR000294	Gamma-carboxyglutamic acid-rich (GLA) domain	Domain
B [auth H]	IPR037111	Thrombin light chain domain superfamily	Homologous Superfamily
B [auth H]	IPR003966	Prothrombin/thrombin	Family
B [auth H]	IPR018056	Kringle, conserved site	Conserved Site
B [auth H]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
B [auth H]	IPR013806	Kringle-like fold	Homologous Superfamily
B [auth H]	IPR038178	Kringle superfamily	Homologous Superfamily
B [auth H]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
B [auth H]	IPR001314	Peptidase S1A, chymotrypsin family	Family
B [auth H]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B [auth H]	IPR001254	Serine proteases, trypsin domain	Domain
B [auth H]	IPR035972	Gamma-carboxyglutamic acid-rich (GLA) domain superfamily	Homologous Superfamily
B [auth H]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
B [auth H]	IPR000001	Kringle	Domain
C [auth I]	IPR005658	Proteinase inhibitor I11, ecotin	Family
C [auth I]	IPR036198	Ecotin superfamily	Homologous Superfamily
C [auth I]	IPR023084	Proteinase inhibitor I11, ecotin, gammaproteobacteria	Family
C [auth I]	IPR027438	Ecotin, C-terminal	Homologous Superfamily