4R8K

Crystal structure of the guinea pig L-asparaginase 1 catalytic domain

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	Glutaminase/Asparaginase	8088909	3001625	SCOP2B (2022-06-29)
B	SCOP2 Family	Glutaminase/Asparaginase	8088908	4000833	SCOP2 (2022-06-29)
B	SCOP2 Superfamily	Glutaminase/Asparaginase	8088909	3001625	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Glutaminase/Asparaginase	8088909	3001625	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Glutaminase/Asparaginase	8088909	3001625	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Glutaminase/Asparaginase	8088909	3001625	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Glutaminase/Asparaginase	8088909	3001625	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Glutaminase/Asparaginase	8088909	3001625	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Glutaminase/Asparaginase	8088909	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	e4r8kA2	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	e4r8kA1	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	e4r8kB1	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	e4r8kB2	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	e4r8kC2	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	e4r8kC1	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)
E	PRK04183	e4r8kE2	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)
E	Asparaginase	e4r8kE1	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)
F	PRK04183	e4r8kF2	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)
F	Asparaginase	e4r8kF1	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)
G	PRK04183	e4r8kG2	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)
G	Asparaginase	e4r8kG1	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)
H	PRK04183	e4r8kH2	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)
H	Asparaginase	e4r8kH1	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	e4r8kD2	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	e4r8kD1	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)
C	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
C	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
E	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
E	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
F	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
F	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
G	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
G	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
H	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
H	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (4.3.0)
D	3.40.50.1170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	L-asparaginase, N-terminal domain	CATH (4.3.0)
D	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, C, D, E A, B, C, D, E, F, G, H	PF00710	Asparaginase, N-terminal (Asparaginase)	Asparaginase, N-terminal	This is the N-terminal domain of this enzyme.	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	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, E A, B, C, D, E, F, G, H	Uncharacterized protein	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	oxoacid metabolic process aspartate family amino acid metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process metabolic process cellular process small molecule metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002110	Ankyrin repeat	Repeat
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027473	L-asparaginase, C-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR041725	Type I (cytosolic) L-asparaginase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR037152	L-asparaginase, N-terminal domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR040919	Asparaginase/glutaminase, C-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027475	Asparaginase/glutaminase, active site 2	Active Site
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036770	Ankyrin repeat-containing domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036152	Asparaginase/glutaminase-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR027474	L-asparaginase, N-terminal	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	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.