2J7C

Beta-glucosidase from Thermotoga maritima in complex with phenylaminomethyl-derived glucoimidazole

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	d2j7cb_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	Family 1 of glycosyl hydrolase	automated matches	(Thermotoga maritima ) [TaxId: 2336 ],	SCOPe (2.08)
A	d2j7ca_	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	(Trans)glycosidases	Family 1 of glycosyl hydrolase	automated matches	(Thermotoga maritima ) [TaxId: 2336 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	(Trans)glycosidases	8043030	3000313	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	(Trans)glycosidases	8043030	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	Glyco_hydro_1	e2j7cB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_1	ECOD (1.6)
A	Glyco_hydro_1	e2j7cA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Glyco_hydro_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)
A	3.20.20.80	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Glycosidases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00232	Glycosyl hydrolase family 1 (Glyco_hydro_1)	Glycosyl hydrolase family 1	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	BETA-GLUCOSIDASE A	hydrolase activity, acting on glycosyl bonds glucosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity beta-glucosidase activity catalytic activity	carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellular process cellulose catabolic process carbohydrate metabolic process catabolic process glucan catabolic process beta-glucan metabolic process carbohydrate catabolic process primary metabolic process macromolecule catabolic process polysaccharide metabolic process glucan metabolic process beta-glucan catabolic process polysaccharide catabolic process metabolic process cellular process cellulose catabolic process macromolecule metabolic process cellulose metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001360	Glycoside hydrolase family 1	Family
A, B	IPR018120	Glycoside hydrolase family 1, active site	Active Site
A, B	IPR017853	Glycoside hydrolase superfamily	Homologous Superfamily
A, B	IPR033132	Glycosyl hydrolases family 1, N-terminal conserved site	Conserved Site
A, B	IPR017736	Glycoside hydrolase, family 1, beta-glucosidase	Family

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.