Annotations: 1EJA

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1ejaa_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d1ejab_	Small proteins	Knottins (small inhibitors, toxins, lectins)	Leech antihemostatic proteins	Huristasin-like	Bdellastasin	medicinal leech (Hirudo medicinalis ) [TaxId: 6421 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Trypsin-like serine proteases	8036522	3000114	SCOP2B (2022-06-29)
B	SCOP2 Family	Huristasin-like	8020338	4003247	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Leech antihemostatic proteins	8032718	3000489	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Trypsin_1	e1ejaA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B	Antistasin	e1ejaB1	A: few secondary structure elements	X: Huristasin-like (From Topology)	H: Huristasin-like (From Topology)	T: Huristasin-like	F: Antistasin	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B	2.10.22.10	Mainly Beta	Ribbon	Antistasin	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
B	PF02822	Antistasin family (Antistasin)	Antistasin family	Members of this family are inhibitors of trypsin family proteases. This domain is highly disulphide bonded. The domain is also found in some large extracellular proteins in multiple copies.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	TRYPSIN	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 metal ion binding small molecule binding	organic substance metabolic process organonitrogen compound metabolic process proteolysis metabolic process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	extracellular region extracellular space cellular anatomical entity
B	BDELLASTASIN	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	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR001254	Serine proteases, trypsin domain	Domain
A	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A	IPR001314	Peptidase S1A, chymotrypsin family	Family
A	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B	IPR004094	Antistasin-like domain	Domain
B	IPR011061	Hirudin/antistatin	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.