1BVN

PIG PANCREATIC ALPHA-AMYLASE IN COMPLEX WITH THE PROTEINACEOUS INHIBITOR TENDAMISTAT

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)
B [auth T]	d1bvnt_	All beta proteins	alpha-Amylase inhibitor tendamistat	alpha-Amylase inhibitor tendamistat	alpha-Amylase inhibitor tendamistat	alpha-Amylase inhibitor tendamistat	(Streptomyces tendae ) [TaxId: 1932 ],	SCOPe (2.08)
A [auth P]	d1bvnp1	All beta proteins	Glycosyl hydrolase domain	Glycosyl hydrolase domain	alpha-Amylases, C-terminal beta-sheet domain	Animal alpha-amylase	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)
A [auth P]	d1bvnp2	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	Amylase, catalytic domain	Animal alpha-amylase	(Sus scrofa ) [TaxId: 9823 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B [auth T]	SCOP2B Superfamily	alpha-amylase inhibitor tendamistat	8037551	3000892	SCOP2B (2022-06-29)
A [auth P]	SCOP2B Superfamily	Glycosyl hydrolase domain-like	8033366	3001528	SCOP2B (2022-06-29)
A [auth P]	SCOP2B Superfamily	(Trans)glycosidases	8033369	3000313	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)
B [auth T]	A_amylase_inhib	e1bvnT1	A: beta sandwiches	X: alpha-Amylase inhibitor tendamistat (From Topology)	H: alpha-Amylase inhibitor tendamistat (From Topology)	T: alpha-Amylase inhibitor tendamistat	F: A_amylase_inhib	ECOD (1.6)
A [auth P]	Alpha-amylase_C	e1bvnP1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: Glycosyl hydrolase domain (From Topology)	T: Glycosyl hydrolase domain	F: Alpha-amylase_C	ECOD (1.6)
A [auth P]	Alpha-amylase	e1bvnP2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Alpha-amylase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth T]	2.60.40.20	Mainly Beta	Sandwich	Immunoglobulin-like	Alpha-amylase inhibitor	CATH (4.3.0)
A [auth P]	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
A [auth P]	2.60.40.1180	Mainly Beta	Sandwich	Immunoglobulin-like	Golgi alpha-mannosidase II	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B [auth T]	PF01356	Alpha amylase inhibitor (A_amylase_inhib)	Alpha amylase inhibitor	-	Domain
A [auth P]	PF00128	Alpha amylase, catalytic domain (Alpha-amylase)	Alpha amylase, catalytic domain	Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, a ...	Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.	Domain
A [auth P]	PF02806	Alpha amylase, C-terminal all-beta domain (Alpha-amylase_C)	Alpha amylase, C-terminal all-beta domain	Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, a ...	Alpha amylase is classified as family 13 of the glycosyl hydrolases. The structure is an 8 stranded alpha/beta barrel containing the active site, interrupted by a ~70 a.a. calcium-binding domain protruding between beta strand 3 and alpha helix 3, and a carboxyl-terminal Greek key beta-barrel domain.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B [auth T]	PROTEIN (TENDAMISTAT)	enzyme regulator activity molecular function inhibitor activity alpha-amylase inhibitor activity molecular function regulator activity enzyme inhibitor activity	-	-
A [auth P]	PROTEIN (ALPHA-AMYLASE)	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding hydrolase activity, acting on glycosyl bonds amylase activity alpha-amylase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity anion binding chloride ion binding	carbohydrate metabolic process catabolic process carbohydrate catabolic process primary metabolic process metabolic process cellular process	cellular anatomical structure extracellular region extracellular space

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B [auth T]	IPR036379	Alpha-amylase inhibitor superfamily	Homologous Superfamily
B [auth T]	IPR000833	Alpha-amylase inhibitor	Family
A [auth P]	IPR006047	Glycosyl hydrolase, family 13, catalytic domain	Domain
A [auth P]	IPR006048	Alpha-amylase/branching enzyme, C-terminal all beta	Domain
A [auth P]	IPR031319	Alpha-amylase, C-terminal domain	Domain
A [auth P]	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A [auth P]	IPR006046	Alpha amylase	Family
A [auth P]	IPR013780	Glycosyl hydrolase, all-beta	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.