2ODY | pdb_00002ody

Thrombin-bound boophilin displays a functional and accessible reactive-site loop

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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)
E	d2odye1	Small proteins	BPTI-like	BPTI-like	automated matches	automated matches	southern cattle tick (Rhipicephalus microplus ) [TaxId: 6941 ],	SCOPe (2.08)
F	d2odyf1	Small proteins	BPTI-like	BPTI-like	automated matches	automated matches	southern cattle tick (Rhipicephalus microplus ) [TaxId: 6941 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
E	Kunitz_BPTI	e2odyE1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)
F	Kunitz_BPTI	e2odyF1	A: few secondary structure elements	X: BPTI-like (From Topology)	H: BPTI-like (From Topology)	T: BPTI-like	F: Kunitz_BPTI	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	4.10.140.10	Few Secondary Structures	Irregular	Epsilon-Thrombin	Chain L	CATH (4.3.0)
C	4.10.140.10	Few Secondary Structures	Irregular	Epsilon-Thrombin	Chain L	CATH (4.3.0)
B	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
D	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
E	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)
F	4.10.410.10	Few Secondary Structures	Irregular	Factor Xa Inhibitor	Pancreatic trypsin inhibitor Kunitz domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, D	PF00089	Trypsin (Trypsin)	Trypsin		Domain
E, F	PF00014	Kunitz/Bovine pancreatic trypsin inhibitor domain (Kunitz_BPTI)	Kunitz/Bovine pancreatic trypsin inhibitor domain	Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the ...	Indicative of a protease inhibitor, usually a serine protease inhibitor. Structure is a disulfide rich alpha+beta fold. BPTI (bovine pancreatic trypsin inhibitor) is an extensively studied model structure. Certain family members are similar to the tick anticoagulant peptide (TAP, Swiss:P17726). This is a highly selective inhibitor of factor Xa in the blood coagulation pathways [1]. TAP molecules are highly dipolar [2], and are arranged to form a twisted two- stranded antiparallel beta-sheet followed by an alpha helix [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	Prothrombin (EC 3.4.21.5)	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 proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery extracellular matrix cellular anatomical structure external encapsulating structure collagen-containing extracellular matrix extracellular region extracellular space
B, D	Prothrombin (EC 3.4.21.5)	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 proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process	cell periphery extracellular matrix cellular anatomical structure external encapsulating structure collagen-containing extracellular matrix extracellular region extracellular space
E, F	Boophilin	enzyme regulator activity peptidase activity peptidase regulator activity catalytic activity, acting on a protein serine hydrolase activity serine-type endopeptidase inhibitor activity hydrolase activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity molecular function inhibitor activity molecular function regulator activity serine-type peptidase activity serine-type endopeptidase activity enzyme regulator activity peptidase activity peptidase regulator activity catalytic activity, acting on a protein serine hydrolase activity serine-type endopeptidase inhibitor activity hydrolase activity enzyme inhibitor activity peptidase inhibitor activity endopeptidase regulator activity endopeptidase inhibitor activity molecular function inhibitor activity molecular function regulator activity serine-type peptidase activity serine-type endopeptidase activity catalytic activity endopeptidase activity toxin activity	biological process involved in interspecies interaction between organisms venom-mediated inhibition of voltage-gated potassium channel activity venom-mediated perturbation of voltage-gated potassium channel activity venom-mediated perturbation of ion channel activity venom-mediated perturbation of biological process modulation of process of another organism	cellular anatomical structure extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR018992	Thrombin light chain	Domain
A, C	IPR000294	Gamma-carboxyglutamic acid-rich (GLA) domain	Domain
A, C	IPR037111	Thrombin light chain domain superfamily	Homologous Superfamily
A, C	IPR051659	Serine Protease S1 Domain-Containing Protein	Family
A, C	IPR003966	Prothrombin/thrombin	Family
A, C	IPR018056	Kringle, conserved site	Conserved Site
A, C	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A, C	IPR013806	Kringle-like fold	Homologous Superfamily
A, C	IPR038178	Kringle superfamily	Homologous Superfamily
A, C	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A, C	IPR001314	Peptidase S1A, chymotrypsin family	Family
A, C	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
A, C	IPR001254	Serine proteases, trypsin domain	Domain
A, C	IPR035972	Gamma-carboxyglutamic acid-rich (GLA) domain superfamily	Homologous Superfamily
A, C	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A, C	IPR000001	Kringle	Domain
B, D	IPR018992	Thrombin light chain	Domain
B, D	IPR000294	Gamma-carboxyglutamic acid-rich (GLA) domain	Domain
B, D	IPR037111	Thrombin light chain domain superfamily	Homologous Superfamily
B, D	IPR051659	Serine Protease S1 Domain-Containing Protein	Family
B, D	IPR003966	Prothrombin/thrombin	Family
B, D	IPR018056	Kringle, conserved site	Conserved Site
B, D	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
B, D	IPR013806	Kringle-like fold	Homologous Superfamily
B, D	IPR038178	Kringle superfamily	Homologous Superfamily
B, D	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
B, D	IPR001314	Peptidase S1A, chymotrypsin family	Family
B, D	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B, D	IPR001254	Serine proteases, trypsin domain	Domain
B, D	IPR035972	Gamma-carboxyglutamic acid-rich (GLA) domain superfamily	Homologous Superfamily
B, D	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
B, D	IPR000001	Kringle	Domain
E, F	IPR002223	Pancreatic trypsin inhibitor Kunitz domain	Domain
E, F	IPR050098	Tissue factor pathway inhibitor/Kunitz-type serine protease inhibitor-like	Family
E, F	IPR020901	Proteinase inhibitor I2, Kunitz, conserved site	Conserved Site
E, F	IPR036880	Pancreatic trypsin inhibitor Kunitz domain superfamily	Homologous Superfamily