3MYW

The Bowman-Birk type inhibitor from mung bean in ternary complex with porcine trypsin

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	d3mywa_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
C [auth B]	d3mywb_	All beta proteins	Trypsin-like serine proteases	Trypsin-like serine proteases	Eukaryotic proteases	Trypsin(ogen)	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
B [auth I]	d3mywi_	Small proteins	Knottins (small inhibitors, toxins, lectins)	Bowman-Birk inhibitor, BBI	Bowman-Birk inhibitor, BBI	automated matches	(Vigna radiata var. radiata ) [TaxId: 3916 ],	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)
C [auth B]	SCOP2B Superfamily	Trypsin-like serine proteases	8036522	3000114	SCOP2B (2022-06-29)
B [auth I]	SCOP2 Family	Bowman-Birk inhibitor, BBI	8070234	4003232	SCOP2 (2022-06-29)
B [auth I]	SCOP2 Superfamily	Bowman-Birk inhibitor, BBI	8070235	3000463	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	e3mywA1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: FMN-binding split barrel 2	F: Trypsin_1	ECOD (1.6)
C [auth B]	Trypsin_1	e3mywB1	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]	Bowman-Birk_leg	e3mywI1	A: few secondary structure elements	X: Bowman-Birk inhibitor, BBI-like (From Topology)	H: Bowman-Birk inhibitor, BBI-like (From Topology)	T: Bowman-Birk inhibitor, BBI-like	F: Bowman-Birk_leg	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)
C [auth B]	2.40.10.10	Mainly Beta	Beta Barrel	Thrombin, subunit H	Trypsin-like serine proteases	CATH (4.3.0)
B [auth I]	2.10.69.10	Mainly Beta	Ribbon	Cysteine Protease (Bromelain) Inhibitor, subunit H	Cysteine Protease (Bromelain) Inhibitor, subunit H	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C [auth B]	PF00089	Trypsin (Trypsin)	Trypsin	-	Domain
B [auth I]	PF00228	Bowman-Birk serine protease inhibitor family (Bowman-Birk_leg)	Bowman-Birk serine protease inhibitor family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C [auth B]	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	proteolysis metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process multicellular organismal process digestion	cellular anatomical structure extracellular region extracellular space
B [auth I]	Bowman-Birk type trypsin inhibitor	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	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 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	cellular anatomical structure extracellular region

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C [auth B]	IPR001254	Serine proteases, trypsin domain	Domain
A, C [auth B]	IPR009003	Peptidase S1, PA clan	Homologous Superfamily
A, C [auth B]	IPR043504	Peptidase S1, PA clan, chymotrypsin-like fold	Homologous Superfamily
A, C [auth B]	IPR050127	Serine Proteases (Peptidase S1 Family)	Family
A, C [auth B]	IPR018114	Serine proteases, trypsin family, histidine active site	Active Site
A, C [auth B]	IPR001314	Peptidase S1A, chymotrypsin family	Family
A, C [auth B]	IPR033116	Serine proteases, trypsin family, serine active site	Active Site
B [auth I]	IPR000877	Proteinase inhibitor I12, Bowman-Birk	Domain
B [auth I]	IPR035995	Bowman-Birk type proteinase inhibitor	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.