Annotations: 1WNF

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1wnfa_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	automated matches	automated matches	(Pyrococcus horikoshii ) [TaxId: 53953 ],	SCOPe (2.08)
B	d1wnfb_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	automated matches	automated matches	(Pyrococcus horikoshii ) [TaxId: 53953 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Glutaminase/Asparaginase	8069755	3001625	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Glutaminase/Asparaginase	8069755	3001625	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	PRK04183	e1wnfA2	A: a/b three-layered sandwiches	X: Glutaminase/Asparaginase C-terminal domain (From Topology)	H: Glutaminase/Asparaginase C-terminal domain (From Topology)	T: Glutaminase/Asparaginase C-terminal domain	F: PRK04183	ECOD (1.6)
A	Asparaginase	e1wnfA3	A: a/b three-layered sandwiches	X: Glutaminase/Asparaginase N-terminal domain (From Topology)	H: Glutaminase/Asparaginase N-terminal domain (From Topology)	T: Glutaminase/Asparaginase N-terminal domain	F: Asparaginase	ECOD (1.6)
B	PRK04183	e1wnfB2	A: a/b three-layered sandwiches	X: Glutaminase/Asparaginase C-terminal domain (From Topology)	H: Glutaminase/Asparaginase C-terminal domain (From Topology)	T: Glutaminase/Asparaginase C-terminal domain	F: PRK04183	ECOD (1.6)
B	Asparaginase	e1wnfB3	A: a/b three-layered sandwiches	X: Glutaminase/Asparaginase N-terminal domain (From Topology)	H: Glutaminase/Asparaginase N-terminal domain (From Topology)	T: Glutaminase/Asparaginase N-terminal domain	F: Asparaginase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
A	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
B	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
B	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00710	Asparaginase, N-terminal (Asparaginase)	Asparaginase, N-terminal	This is the N-terminal domain of this enzyme.	Domain
A, B	PF17763	Glutaminase/Asparaginase C-terminal domain (Asparaginase_C)	Glutaminase/Asparaginase C-terminal domain	This domain is found at the C-terminus of asparaginase enzymes.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	L-asparaginase	asparaginase 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	organic substance metabolic process amino acid metabolic process primary metabolic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR027473	L-asparaginase, C-terminal	Homologous Superfamily
A, B	IPR041725	Type I (cytosolic) L-asparaginase	Family
A, B	IPR037152	L-asparaginase, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR040919	Asparaginase/glutaminase, C-terminal	Domain
A, B	IPR027475	Asparaginase/glutaminase, active site 2	Active Site
A, B	IPR006033	Type I L-asparaginase family	Family
A, B	IPR036152	Asparaginase/glutaminase-like superfamily	Homologous Superfamily
A, B	IPR027474	L-asparaginase, N-terminal	Domain
A, B	IPR006034	Asparaginase/glutaminase-like	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.