3CEV

ARGINASE FROM BACILLUS CALDEVELOX, COMPLEXED WITH L-ARGININE

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3ceva_	Alpha and beta proteins (a/b)	Arginase/deacetylase	Arginase/deacetylase	Arginase-like amidino hydrolases	Arginase	([Bacillus] caldovelox ) [TaxId: 33931 ],	SCOPe (2.08)
B	d3cevb_	Alpha and beta proteins (a/b)	Arginase/deacetylase	Arginase/deacetylase	Arginase-like amidino hydrolases	Arginase	([Bacillus] caldovelox ) [TaxId: 33931 ],	SCOPe (2.08)
C	d3cevc_	Alpha and beta proteins (a/b)	Arginase/deacetylase	Arginase/deacetylase	Arginase-like amidino hydrolases	Arginase	([Bacillus] caldovelox ) [TaxId: 33931 ],	SCOPe (2.08)
D	d3cevd_	Alpha and beta proteins (a/b)	Arginase/deacetylase	Arginase/deacetylase	Arginase-like amidino hydrolases	Arginase	([Bacillus] caldovelox ) [TaxId: 33931 ],	SCOPe (2.08)
E	d3ceve_	Alpha and beta proteins (a/b)	Arginase/deacetylase	Arginase/deacetylase	Arginase-like amidino hydrolases	Arginase	([Bacillus] caldovelox ) [TaxId: 33931 ],	SCOPe (2.08)
F	d3cevf_	Alpha and beta proteins (a/b)	Arginase/deacetylase	Arginase/deacetylase	Arginase-like amidino hydrolases	Arginase	([Bacillus] caldovelox ) [TaxId: 33931 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Arginase/deacetylase-like	8044334	3000260	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Arginase/deacetylase-like	8044334	3000260	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Arginase/deacetylase-like	8044334	3000260	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Arginase/deacetylase-like	8044334	3000260	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Arginase/deacetylase-like	8044334	3000260	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Arginase/deacetylase-like	8044334	3000260	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	Arginase	e3cevA1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: Arginase/deacetylase	F: Arginase	ECOD (1.6)
B	Arginase	e3cevB1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: Arginase/deacetylase	F: Arginase	ECOD (1.6)
C	Arginase	e3cevC1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: Arginase/deacetylase	F: Arginase	ECOD (1.6)
D	Arginase	e3cevD1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: Arginase/deacetylase	F: Arginase	ECOD (1.6)
E	Arginase	e3cevE1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: Arginase/deacetylase	F: Arginase	ECOD (1.6)
F	Arginase	e3cevF1	A: a/b three-layered sandwiches	X: HAD domain-like	H: HAD domain-related	T: Arginase/deacetylase	F: Arginase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.800.10	Alpha Beta	3-Layer(aba) Sandwich	Arginase	Chain A	CATH (4.3.0)
B	3.40.800.10	Alpha Beta	3-Layer(aba) Sandwich	Arginase	Chain A	CATH (4.3.0)
C	3.40.800.10	Alpha Beta	3-Layer(aba) Sandwich	Arginase	Chain A	CATH (4.3.0)
D	3.40.800.10	Alpha Beta	3-Layer(aba) Sandwich	Arginase	Chain A	CATH (4.3.0)
E	3.40.800.10	Alpha Beta	3-Layer(aba) Sandwich	Arginase	Chain A	CATH (4.3.0)
F	3.40.800.10	Alpha Beta	3-Layer(aba) Sandwich	Arginase	Chain A	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	PF00491	Arginase family (Arginase)	Arginase family	-	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	PROTEIN (ARGINASE)	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds arginase activity cation binding ion binding binding metal ion binding small molecule binding	organonitrogen compound metabolic process organonitrogen compound biosynthetic process amide biosynthetic process urea metabolic process nitrogen cycle metabolic process organic substance metabolic process biosynthetic process urea cycle organic substance biosynthetic process small molecule metabolic process metabolic process amide metabolic process oxoacid metabolic process cellular metabolic process organonitrogen compound metabolic process organonitrogen compound biosynthetic process amide biosynthetic process urea metabolic process nitrogen cycle metabolic process organic substance metabolic process biosynthetic process urea cycle organic substance biosynthetic process small molecule metabolic process metabolic process amide metabolic process oxoacid metabolic process cellular metabolic process carboxylic acid metabolic process amino acid metabolic process primary metabolic process organic acid metabolic process alpha-amino acid metabolic process arginine metabolic process cellular process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR014033	Arginase	Family
A, B, C, D, E A, B, C, D, E, F	IPR020855	Ureohydrolase, manganese-binding site	Binding Site
A, B, C, D, E A, B, C, D, E, F	IPR023696	Ureohydrolase domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR006035	Ureohydrolase	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.