Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyMetallo-dependent hydrolases8043396 3000428 SCOP2B (2022-06-29)
BSCOP2B SuperfamilyMetallo-dependent hydrolases8043396 3000428 SCOP2B (2022-06-29)
CSCOP2B SuperfamilyMetallo-dependent hydrolases8043396 3000428 SCOP2B (2022-06-29)
DSCOP2B SuperfamilyMetallo-dependent hydrolases8043396 3000428 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
APF00962e1a4lA1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00962ECOD (1.6)
BPF00962e1a4lB1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00962ECOD (1.6)
CPF00962e1a4lC1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00962ECOD (1.6)
DPF00962e1a4lD1 A: a/b barrelsX: TIM beta/alpha-barrelH: TIM barrels (From Topology)T: TIM barrelsF: PF00962ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A3.20.20.140 Alpha Beta Alpha-Beta Barrel TIM Barrel Metal-dependent hydrolasesCATH (4.3.0)
B3.20.20.140 Alpha Beta Alpha-Beta Barrel TIM Barrel Metal-dependent hydrolasesCATH (4.3.0)
C3.20.20.140 Alpha Beta Alpha-Beta Barrel TIM Barrel Metal-dependent hydrolasesCATH (4.3.0)
D3.20.20.140 Alpha Beta Alpha-Beta Barrel TIM Barrel Metal-dependent hydrolasesCATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B, C, D
PF00962Adenosine deaminase (A_deaminase)Adenosine deaminase- Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B, C, D
ADENOSINE DEAMINASE

InterPro: Protein Family Classification InterPro Database Homepage

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
adenosine deaminase  M-CSA #376

Adenosine deaminase (ADA) is the critical enzyme in purine metabolism, which catalyses the irreversible deamination of adenosine and deoxyadenosine to their respective inosine product. It is present in virtually all mammalian cells and has a central role in maintaining immune competence. Genetic deficiency of ADA in humans is associated with severe combined immunodeficiency disease, whereas abnormally high level of ADA is involved in a variety of other diseases including acquired immunodeficiency syndrome (AIDS), tuberculosis, Parkinson's disease, anemia, various lymphomas and leukemias. ADA is therefore regarded as an important therapeutic target and the detailed knowledge of its catalytic mechanism is of high significance in drug design.

Defined by 6 residues: HIS:A-12 [auth A-15]HIS:A-14 [auth A-17]HIS:A-211 [auth A-214]GLU:A-214 [auth A-217]HIS:A-235 [auth A-238]ASP:A-292 [auth A-295]
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