3UT0

Crystal structure of exo-1,3/1,4-beta-glucanase (EXOP) from Pseudoalteromonas sp. BB1

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF18559	e3ut0A3	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: PF18559	ECOD (1.6)
A	PF00933	e3ut0A1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
A	PF01915	e3ut0A2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)
B	PF18559	e3ut0B3	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: PF18559	ECOD (1.6)
B	PF00933	e3ut0B1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
B	PF01915	e3ut0B2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)
C	PF18559	e3ut0C3	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: PF18559	ECOD (1.6)
C	PF00933	e3ut0C1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
C	PF01915	e3ut0C2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)
D	PF18559	e3ut0D3	A: beta sandwiches	X: jelly-roll	H: Concanavalin A-like	T: Galactose-binding domain-like	F: PF18559	ECOD (1.6)
D	PF00933	e3ut0D1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00933	ECOD (1.6)
D	PF01915	e3ut0D2	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Beta-D-glucan exohydrolase, C-terminal domain (From Topology)	T: Beta-D-glucan exohydrolase, C-terminal domain	F: PF01915	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
A	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
A	2.60.120.430	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding lectin	CATH (4.3.0)
B	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
B	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
B	2.60.120.430	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding lectin	CATH (4.3.0)
C	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
C	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
C	2.60.120.430	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding lectin	CATH (4.3.0)
D	3.20.20.300	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycoside hydrolase, family 3, N-terminal domain	CATH (4.3.0)
D	3.40.50.1700	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Glycoside hydrolase family 3 C-terminal domain	CATH (4.3.0)
D	2.60.120.430	Mainly Beta	Sandwich	Jelly Rolls	Galactose-binding lectin	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00933	Glycosyl hydrolase family 3 N terminal domain (Glyco_hydro_3)	Glycosyl hydrolase family 3 N terminal domain	-	Domain
A, B, C, D	PF01915	Glycosyl hydrolase family 3 C-terminal domain (Glyco_hydro_3_C)	Glycosyl hydrolase family 3 C-terminal domain	This domain is involved in catalysis and may be involved in binding beta-glucan [1]. This domain is found associated with Pfam:PF00933.	Domain
A, B, C, D	PF18559	Galactose-binding domain-like (Exop_C)	Galactose-binding domain-like	This is the C-terminal domain found in ExoP (exo-1,3/1,4-beta-glucanase) from Pseudoalteromonas. This domain contains a beta-sandwich fold which is common in glycosyl hydrolases (GH7, 11, 12 and 16) and in some 23 carbohydrate-binding modules. It is ...	This is the C-terminal domain found in ExoP (exo-1,3/1,4-beta-glucanase) from Pseudoalteromonas. This domain contains a beta-sandwich fold which is common in glycosyl hydrolases (GH7, 11, 12 and 16) and in some 23 carbohydrate-binding modules. It is suggested that the main role of this domain is to provide structural stability necessary for ExoP activity, however no substrate-binding role has been shown [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Exo-1,3/1,4-beta-glucanase	hydrolase activity, acting on glycosyl bonds hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity catalytic activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process organic substance metabolic process primary metabolic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR001764	Glycoside hydrolase, family 3, N-terminal	Domain
A, B, C, D	IPR036962	Glycoside hydrolase, family 3, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B, C, D	IPR041443	ExoP, galactose-binding-like domain	Domain
A, B, C, D	IPR036881	Glycoside hydrolase family 3 C-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR002772	Glycoside hydrolase family 3 C-terminal 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 R01GM133198.