Annotations: 8ECE

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Glutaminase/Asparaginase	8033474	3001625	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Glutaminase/Asparaginase	8033474	3001625	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Glutaminase/Asparaginase	8033474	3001625	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Glutaminase/Asparaginase	8033474	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	e8eceA2	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	e8eceA1	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	e8eceB2	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	e8eceB1	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)
C	PRK04183	e8eceC1	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)
C	Asparaginase	e8eceC2	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)
D	PRK04183	e8eceD1	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)
D	Asparaginase	e8eceD2	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00710	Asparaginase, N-terminal (Asparaginase)	Asparaginase, N-terminal	This is the N-terminal domain of this enzyme.	Domain
A, B, C, D	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, C, D	L-asparaginase 2	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 identical protein binding protein binding binding	catabolic process oxoacid metabolic process glutamine family amino acid catabolic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process organic acid catabolic process asparagine catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process catabolic process oxoacid metabolic process glutamine family amino acid catabolic process aspartate family amino acid metabolic process amino acid metabolic process organic acid metabolic process organic acid catabolic process asparagine catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process carboxylic acid catabolic process small molecule metabolic process amino acid catabolic process aspartate family amino acid catabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process asparagine metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process protein-containing complex organization protein homotetramerization cellular component organization cellular component biogenesis cellular component assembly protein complex oligomerization protein tetramerization protein-containing complex assembly protein homooligomerization cellular component organization or biogenesis	cellular anatomical structure periplasmic space outer membrane-bounded periplasmic space cell envelope protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR027473	L-asparaginase, C-terminal	Homologous Superfamily
A, B, C, D	IPR027475	Asparaginase/glutaminase, active site 2	Active Site
A, B, C, D	IPR036152	Asparaginase/glutaminase-like superfamily	Homologous Superfamily
A, B, C, D	IPR020827	Asparaginase/glutaminase, active site 1	Active Site
A, B, C, D	IPR037152	L-asparaginase, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D	IPR040919	Asparaginase/glutaminase, C-terminal	Domain
A, B, C, D	IPR027474	L-asparaginase, N-terminal	Domain
A, B, C, D	IPR004550	L-asparaginase, type II	Family
A, B, C, D	IPR006034	Asparaginase/glutaminase-like	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.