6V28

Complex of double mutant (T89V,K162T) of E. coli L-asparaginase II with L-Asp

External Resource: Annotation

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6v28a_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Asparaginase type II	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d6v28b_	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Asparaginase type II	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d6v28c1	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Asparaginase type II	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d6v28c2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
D	d6v28d1	Alpha and beta proteins (a/b)	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Glutaminase/Asparaginase	Asparaginase type II	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
D	d6v28d2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Escherichia coli K-12 ) [TaxId: 83333 ],	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	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	e6v28A1	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	e6v28A2	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	e6v28B2	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	e6v28B1	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	e6v28C1	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	e6v28C2	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	e6v28D1	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	e6v28D2	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 (utative)
A	3.40.50.40	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold		CATH (utative)

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 cellular metabolic 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	periplasmic space cellular anatomical entity 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

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	AEI	Parent Component: THR RESID: AA0525 PSI-MOD : O-(L-isoaspartyl)-L-threonine (active site intermediate) MOD:01671 , O-(L-isoaspartyl)-L-threonine (cross-link) MOD:01947

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.