1ACB

CRYSTAL AND MOLECULAR STRUCTURE OF THE BOVINE ALPHA-CHYMOTRYPSIN-EGLIN C COMPLEX AT 2.0 ANGSTROMS RESOLUTION

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 E]	d1acbe_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	(alpha,gamma)-chymotrypsin(ogen)	Bovine (Bos taurus ) [TaxId: 9913 ],	SCOPe (2.08)
B [auth I]	d1acbi_	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	Eglin C	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 [auth E]	SCOP2B Superfamily	Trypsin-like serine proteases	8042128	3000114	SCOP2B (2022-06-29)
B [auth I]	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)
A [auth E]	Trypsin_1	e1acbE1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
B [auth I]	potato_inhibit	e1acbI1	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)
A [auth E]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B [auth I]	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 [auth E]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
B [auth I]	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 [auth E]	ALPHA-CHYMOTRYPSIN	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 binding binding serpin family protein 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
B [auth I]	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 negative regulation of hydrolase activity negative regulation of proteolysis regulation of cellular process regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity regulation of primary metabolic process negative regulation of peptidase activity regulation of proteolysis proteolysis negative regulation of cellular process response to stimulus response to stress response to wounding negative regulation of hydrolase activity negative regulation of proteolysis regulation of cellular process regulation of catalytic activity negative regulation of biological process negative regulation of catalytic activity regulation of primary metabolic process negative regulation of peptidase activity regulation of proteolysis proteolysis negative regulation of cellular process protein metabolic process negative regulation of protein metabolic process negative regulation of macromolecule metabolic process regulation of biological process regulation of protein metabolic process negative regulation of metabolic process biological regulation negative regulation of molecular function regulation of peptidase activity primary metabolic process regulation of macromolecule metabolic process regulation of molecular function regulation of hydrolase activity metabolic process cellular process macromolecule metabolic process regulation of metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth E]	IPR001254	Serine proteases, trypsin domain	Domain
A [auth E]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A [auth E]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A [auth E]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A [auth E]	IPR001314	Peptidase S1A, chymotrypsin family	Family
A [auth E]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B [auth I]	IPR000864	Proteinase inhibitor I13, potato inhibitor I	Family
B [auth I]	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.