6WYX

Crystal structure of Pseudomonas 7A Glutaminase-Asparaginase in complex with L-Asp at pH 5.0

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6wyxa_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
B	d6wyxb_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
C	d6wyxc_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	SCOPe (2.08)
D	d6wyxd_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	automated matches	(Pseudomonas putida KT2440 ) [TaxId: 160488 ],	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	8100082	3001625	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Glutaminase/Asparaginase	8100082	3001625	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Glutaminase/Asparaginase	8100082	3001625	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Glutaminase/Asparaginase	8100082	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	e6wyxA1	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	e6wyxA2	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	e6wyxB2	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	e6wyxB1	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	e6wyxC1	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	e6wyxC2	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	e6wyxD2	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	e6wyxD1	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	Glutaminase-asparaginase	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 glutamin-(asparagin-)ase activity glutaminase activity asparaginase activity amidase activity	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 asparagine metabolic process metabolic process cellular process small molecule metabolic process	cellular anatomical structure periplasmic space

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.