5MHF

Murine endoplasmic reticulum alpha-glucosidase I with N-9'-methoxynonyl-1-deoxynojirimycin.

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Glyco_hydro_63_N	e5mhfA1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_hydro_63_N	ECOD (1.6)
A	Glyco_hydro_63	e5mhfA2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_63	ECOD (1.6)
B	Glyco_hydro_63_N	e5mhfB2	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_hydro_63_N	ECOD (1.6)
B	Glyco_hydro_63	e5mhfB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_63	ECOD (1.6)
C	Glyco_hydro_63_N	e5mhfC1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_hydro_63_N	ECOD (1.6)
C	Glyco_hydro_63	e5mhfC2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_63	ECOD (1.6)
D	Glyco_hydro_63_N	e5mhfD1	A: beta sandwiches	X: Glycosyl hydrolase domain-like	H: supersandwich (From Topology)	T: supersandwich	F: Glyco_hydro_63_N	ECOD (1.6)
D	Glyco_hydro_63	e5mhfD2	A: alpha superhelices	X: Repetitive alpha hairpins	H: alpha/alpha toroid (From Topology)	T: alpha/alpha toroid	F: Glyco_hydro_63	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF03200	Glycosyl hydrolase family 63 C-terminal domain (Glyco_hydro_63)	Glycosyl hydrolase family 63 C-terminal domain	-	Repeat
A, B, C, D	PF16923	Glycosyl hydrolase family 63 N-terminal domain (Glyco_hydro_63N)	Glycosyl hydrolase family 63 N-terminal domain	This is a family of eukaryotic enzymes belonging to glycosyl hydrolase family 63. They catalyse the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC:3.2.1.106 is the f ...	This is a family of eukaryotic enzymes belonging to glycosyl hydrolase family 63. They catalyse the specific cleavage of the non-reducing terminal glucose residue from Glc(3)Man(9)GlcNAc(2). Mannosyl oligosaccharide glucosidase EC:3.2.1.106 is the first enzyme in the N-linked oligosaccharide processing pathway. This family represents the N-terminal beta sandwich domain [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Mannosyl-oligosaccharide glucosidase	alpha-glucosidase activity hydrolase activity, acting on glycosyl bonds glucosidase activity hydrolase activity, hydrolyzing O-glycosyl compounds hydrolase activity Glc3Man9GlcNAc2 oligosaccharide glucosidase activity catalytic activity	carbohydrate derivative biosynthetic process cellular biosynthetic process cellular metabolic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein N-linked glycosylation protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation carbohydrate derivative biosynthetic process cellular biosynthetic process cellular metabolic process glycoprotein biosynthetic process carbohydrate derivative metabolic process primary metabolic process glycoprotein metabolic process protein N-linked glycosylation protein glycosylation macromolecule biosynthetic process biosynthetic process glycosylation macromolecule modification macromolecule glycosylation metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process carbohydrate metabolic process oligosaccharide metabolic process	membrane-bounded organelle intracellular anatomical structure organelle subcompartment membrane cellular anatomical entity intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cytoplasm organelle membrane membrane-bounded organelle intracellular anatomical structure organelle subcompartment membrane cellular anatomical entity intracellular membrane-bounded organelle endomembrane system endoplasmic reticulum subcompartment intracellular organelle organelle nuclear outer membrane-endoplasmic reticulum membrane network endoplasmic reticulum cytoplasm organelle membrane endoplasmic reticulum membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR012341	Six-hairpin glycosidase-like superfamily	Homologous Superfamily
A, B, C, D	IPR031335	Glycosyl hydrolase family 63, C-terminal	Domain
A, B, C, D	IPR004888	Glycoside hydrolase family 63	Family
A, B, C, D	IPR008928	Six-hairpin glycosidase superfamily	Homologous Superfamily
A, B, C, D	IPR038518	Glycosyl hydrolase family 63, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR031631	Glycosyl hydrolase family 63, N-terminal	Domain

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	MLY	Parent Component: LYS RESID: AA0075 PSI-MOD : N6,N6-dimethyl-L-lysine MOD:00084
A, B, C, D	SME	Parent Component: MET RESID: AA0075 , AA0581 PSI-MOD : N6,N6-dimethyl-L-lysine MOD:00084 , L-methionine (S)-sulfoxide MOD:00721

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.