1EAI | pdb_00001eai

COMPLEX OF ASCARIS CHYMOTRPSIN/ELASTASE INHIBITOR WITH PORCINE ELASTASE

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	d1eaia_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Elastase	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B	d1eaib_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Elastase	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
C	d1eaic_	Small proteins	Serine protease inhibitors	Serine protease inhibitors	ATI-like	Ascaris elastase inhibitor	(Ascaris suum ) [TaxId: 6253 ],	SCOPe (2.08)
D	d1eaid_	Small proteins	Serine protease inhibitors	Serine protease inhibitors	ATI-like	Ascaris elastase inhibitor	(Ascaris suum ) [TaxId: 6253 ],	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	8039111	3000114	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Trypsin-like serine proteases	8039111	3000114	SCOP2B (2022-06-29)
C	SCOP2 Family	ATI-like	8026507	4003491	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Serine protease inhibitors	8038886	3000944	SCOP2 (2022-06-29)
D	SCOP2B Superfamily	Serine protease inhibitors	8038886	3000944	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)
A	Trypsin_1	e1eaiA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B	Trypsin_1	e1eaiB1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
C	TIL	e1eaiC1	A: few secondary structure elements	X: EGF-like	H: Serine protease inhibitors (From Topology)	T: Serine protease inhibitors	F: TIL	ECOD (1.6)
D	TIL	e1eaiD1	A: few secondary structure elements	X: EGF-like	H: Serine protease inhibitors (From Topology)	T: Serine protease inhibitors	F: TIL	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	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
C	2.10.25.10	Mainly Beta	Ribbon	Laminin	Laminin	CATH (4.3.0)
D	2.10.25.10	Mainly Beta	Ribbon	Laminin	Laminin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00089	Trypsin (Trypsin)	Trypsin		Domain
C, D	PF01826	Trypsin Inhibitor like cysteine rich domain (TIL)	Trypsin Inhibitor like cysteine rich domain	This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, ...	This family contains trypsin inhibitors as well as a domain found in many extracellular proteins. The domain typically contains ten cysteine residues that form five disulphide bonds. The cysteine residues that form the disulphide bonds are 1-7, 2-6, 3-5, 4-10 and 8-9.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (ELASTASE)	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	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process	cellular anatomical structure extracellular region extracellular space
C, D	PROTEIN (CHYMOTRYPSIN/ELASTASE ISOINHIBITOR 1)	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	-	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001254	Serine proteases, trypsin domain	Domain
A, B	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A, B	IPR050850	Peptidase S1 family, Elastase subfamily	Family
A, B	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A, B	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A, B	IPR001314	Peptidase S1A, chymotrypsin family	Family
A, B	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
C, D	IPR036084	Serine protease inhibitor-like superfamily	Homologous Superfamily
C, D	IPR002919	Trypsin Inhibitor-like, cysteine rich domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), 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 R01GM157729.