3PBM

The crystal structure of adenosine deaminase in complex with chloropurine from Pseudomonas aeruginosa

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	Metallo-dependent hydrolases	8071774	3000428	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metallo-dependent hydrolases	8071774	3000428	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	A_deaminase	e3pbmA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: A_deaminase	ECOD (1.6)
B	A_deaminase	e3pbmB1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: A_deaminase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)
B	3.20.20.140	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Metal-dependent hydrolases	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00962	Adenosine deaminase (A_deaminase)	Adenosine deaminase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Adenosine deaminase	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines adenine deaminase activity hydrolase activity catalytic activity deaminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	catabolic process purine nucleobase metabolic process primary metabolic process purine-containing compound catabolic process purine nucleobase catabolic process purine-containing compound metabolic process adenine catabolic process nucleobase-containing compound metabolic process nucleobase catabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process adenine metabolic process small molecule metabolic process metabolic process catabolic process purine nucleobase metabolic process primary metabolic process purine-containing compound catabolic process purine nucleobase catabolic process purine-containing compound metabolic process adenine catabolic process nucleobase-containing compound metabolic process nucleobase catabolic process nucleobase-containing small molecule metabolic process nucleobase metabolic process adenine metabolic process small molecule metabolic process metabolic process cellular process nucleoside phosphate metabolic process nucleotide metabolic process organophosphate metabolic process phosphate-containing compound metabolic process phosphorus metabolic process purine-containing compound salvage nucleobase biosynthetic process purine nucleobase biosynthetic process hypoxanthine biosynthetic process hypoxanthine metabolic process biosynthetic process purine-containing compound biosynthetic process hypoxanthine salvage purine nucleobase salvage cellular metabolic compound salvage	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001365	Adenosine deaminase domain	Domain
A, B	IPR006330	Adenosine/adenine deaminase	Family
A, B	IPR028892	Adenine deaminase type 2	Family
A, B	IPR032466	Metal-dependent hydrolase	Homologous Superfamily

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.