Annotations: 2GAW

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2gaw.1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	(Glycosyl)asparaginase	Glycosylasparaginase (aspartylglucosaminidase, AGA)	(Elizabethkingia meningoseptica ) [TaxId: 238 ],	SCOPe (2.08)
C	d2gaw.2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	(Glycosyl)asparaginase	Glycosylasparaginase (aspartylglucosaminidase, AGA)	(Elizabethkingia meningoseptica ) [TaxId: 238 ],	SCOPe (2.08)
B	d2gaw.1	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	(Glycosyl)asparaginase	Glycosylasparaginase (aspartylglucosaminidase, AGA)	(Elizabethkingia meningoseptica ) [TaxId: 238 ],	SCOPe (2.08)
D	d2gaw.2	Alpha and beta proteins (a+b)	Ntn hydrolase-like	N-terminal nucleophile aminohydrolases (Ntn hydrolases)	(Glycosyl)asparaginase	Glycosylasparaginase (aspartylglucosaminidase, AGA)	(Elizabethkingia meningoseptica ) [TaxId: 238 ],	SCOPe (2.08)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.60.20.30	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	(Glycosyl)asparaginase	CATH (4.3.0)
D	3.60.20.30	Alpha Beta	4-Layer Sandwich	Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1	(Glycosyl)asparaginase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C	PF01112	Asparaginase (Asparaginase_2)	Asparaginase	-	Domain
B, D	PF01112	Asparaginase (Asparaginase_2)	Asparaginase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C	GLYCOSYLASPARAGINASE	asparaginase activity amidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity peptidase activity omega peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity beta-aspartyl-peptidase activity	macromolecule modification protein deglycosylation carbohydrate derivative metabolic process metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process glycoprotein metabolic process proteolysis	cellular anatomical structure periplasmic space intracellular anatomical structure cytoplasm
B, D	GLYCOSYLASPARAGINASE	asparaginase activity amidase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity peptidase activity omega peptidase activity catalytic activity, acting on a protein threonine-type peptidase activity beta-aspartyl-peptidase activity	macromolecule modification protein deglycosylation carbohydrate derivative metabolic process metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process glycoprotein metabolic process proteolysis	cellular anatomical structure periplasmic space intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
A, C	IPR000246	Peptidase T2, asparaginase 2	Family
A, C	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal	Conserved Site
B, D	IPR029055	Nucleophile aminohydrolases, N-terminal	Homologous Superfamily
B, D	IPR000246	Peptidase T2, asparaginase 2	Family
B, D	IPR019546	Twin-arginine translocation pathway, signal sequence, bacterial/archaeal	Conserved Site

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.