5FJS

Bacterial beta-glucosidase reveals the structural and functional basis of genetic defects in human glucocerebrosidase 2 (GBA2)

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Six-hairpin glycosidases	8051855	3000970	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Galactose mutarotase-like	8051856	3000035	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Six-hairpin glycosidases	8051855	3000970	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	Glyco_hydr_116N	e5fjsA2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_hydr_116N	ECOD (1.6)
A	DUF608	e5fjsA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: DUF608	ECOD (1.6)
B	Glyco_hydr_116N	e5fjsB2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_hydr_116N	ECOD (1.6)
B	DUF608	e5fjsB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: DUF608	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF12215	beta-glucosidase 2, glycosyl-hydrolase family 116 N-term (Glyco_hydr_116N)	beta-glucosidase 2, glycosyl-hydrolase family 116 N-term	-	Family
A, B	PF04685	Glycosyl-hydrolase family 116, catalytic region (DUF608)	Glycosyl-hydrolase family 116, catalytic region	-	Repeat

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GLUCOSYLCERAMIDASE	hydrolase activity, acting on glycosyl bonds glucosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity beta-glucosidase activity catalytic activity glucosylceramidase activity glycosylceramidase activity cation binding ion binding binding metal ion binding small molecule binding	carbohydrate metabolic process primary metabolic process metabolic process cellular process sphingolipid catabolic process catabolic process glycolipid metabolic process carbohydrate derivative metabolic process ceramide catabolic process amide metabolic process glycosylceramide metabolic process membrane lipid metabolic process ceramide metabolic process carbohydrate derivative catabolic process carbohydrate metabolic process primary metabolic process metabolic process cellular process sphingolipid catabolic process catabolic process glycolipid metabolic process carbohydrate derivative metabolic process ceramide catabolic process amide metabolic process glycosylceramide metabolic process membrane lipid metabolic process ceramide metabolic process carbohydrate derivative catabolic process glycosphingolipid catabolic process lipid catabolic process glycosphingolipid metabolic process liposaccharide metabolic process sphingolipid metabolic process glucosylceramide metabolic process membrane lipid catabolic process glycosylceramide catabolic process glycolipid catabolic process glucosylceramide catabolic process lipid metabolic process	cellular anatomical structure membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A, B	IPR014551	Beta-glucosidase GBA2-type	Family
A, B	IPR024462	Glycosyl-hydrolase family 116, N-terminal	Domain
A, B	IPR052566	Non-lysosomal glucosylceramidase	Family
A, B	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
A, B	IPR006775	Glycosyl-hydrolase family 116, catalytic region	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 R01GM157729.