4B2C

Structure of the factor Xa-like trypsin variant triple-Ala (TPA) in complex with eglin C

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)
C	d4b2cc_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	CATTLE (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
A	d4b2ca_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	CATTLE (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B	d4b2cb1	Alpha and beta proteins (a+b)	CI-2 family of serine protease inhibitors	CI-2 family of serine protease inhibitors	CI-2 family of serine protease inhibitors	automated matches	MEDICINAL LEECH (Hirudo medicinalis ) [TaxId: 6421 ],	SCOPe (2.08)
B	d4b2cb2	Artifacts	Tags	Tags	Tags	N-terminal Tags	MEDICINAL LEECH (Hirudo medicinalis ) [TaxId: 6421 ],	SCOPe (2.08)
D	d4b2cd1	Alpha and beta proteins (a+b)	CI-2 family of serine protease inhibitors	CI-2 family of serine protease inhibitors	CI-2 family of serine protease inhibitors	automated matches	MEDICINAL LEECH (Hirudo medicinalis ) [TaxId: 6421 ],	SCOPe (2.08)
D	d4b2cd2	Artifacts	Tags	Tags	Tags	N-terminal Tags	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)
C	SCOP2B Superfamily	Trypsin-like serine proteases	8037496	3000114	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Trypsin-like serine proteases	8037496	3000114	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	CI-2 serine protease inhibitor-like	8034986	3000827	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	CI-2 serine protease inhibitor-like	8034986	3000827	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	Trypsin_1	e4b2cC1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
A	Trypsin_1	e4b2cA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B	potato_inhibit	e4b2cB1	A: a+b two layers	X: CI-2 family of serine protease inhibitors-like	H: CI-2 family of serine protease inhibitors (From Topology)	T: CI-2 family of serine protease inhibitors	F: potato_inhibit	ECOD (1.6)
D	potato_inhibit	e4b2cD1	A: a+b two layers	X: CI-2 family of serine protease inhibitors-like	H: CI-2 family of serine protease inhibitors (From Topology)	T: CI-2 family of serine protease inhibitors	F: potato_inhibit	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
A	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B	3.30.10.10	Alpha Beta	2-Layer Sandwich	Trypsin Inhibitor V	Chain A	CATH (4.3.0)
D	3.30.10.10	Alpha Beta	2-Layer Sandwich	Trypsin Inhibitor V	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
B, D	PF00280	Potato inhibitor I family (potato_inhibit)	Potato inhibitor I family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	CATIONIC TRYPSIN	peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity protein binding binding serpin family protein binding cation binding ion binding metal ion binding peptidase activity catalytic activity, acting on a protein hydrolase activity catalytic activity endopeptidase activity serine hydrolase activity serine-type peptidase activity serine-type endopeptidase activity protein binding binding serpin family protein binding cation binding ion binding metal ion binding small molecule binding	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	protein-containing complex serine protease inhibitor complex protease inhibitor complex peptidase inhibitor complex cellular anatomical structure extracellular region extracellular space
B, D	EGLIN C	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	response to stimulus response to stress response to wounding	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
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	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A, C	IPR050127	Serine Proteases (Peptidase S1 Family)	Family
A, C	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
B, D	IPR000864	Proteinase inhibitor I13, potato inhibitor I	Family
B, D	IPR036354	Proteinase inhibitor I13, potato inhibitor I superfamily	Homologous Superfamily

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.