1A4L
ADA STRUCTURE COMPLEXED WITH DEOXYCOFORMYCIN AT PH 7.0
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
D | d1a4ld_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Metallo-dependent hydrolases | Adenosine/AMP deaminase | Adenosine deaminase (ADA) | house mouse (Mus musculus ) [TaxId: 10090 ], | SCOPe (2.08) |
A | d1a4la_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Metallo-dependent hydrolases | Adenosine/AMP deaminase | Adenosine deaminase (ADA) | house mouse (Mus musculus ) [TaxId: 10090 ], | SCOPe (2.08) |
B | d1a4lb_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Metallo-dependent hydrolases | Adenosine/AMP deaminase | Adenosine deaminase (ADA) | house mouse (Mus musculus ) [TaxId: 10090 ], | SCOPe (2.08) |
C | d1a4lc_ | Alpha and beta proteins (a/b) | TIM beta/alpha-barrel | Metallo-dependent hydrolases | Adenosine/AMP deaminase | Adenosine deaminase (ADA) | house mouse (Mus musculus ) [TaxId: 10090 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
D | SCOP2B Superfamily | Metallo-dependent hydrolases | 8043396 | 3000428 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | Metallo-dependent hydrolases | 8043396 | 3000428 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | Metallo-dependent hydrolases | 8043396 | 3000428 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | Metallo-dependent hydrolases | 8043396 | 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) |
---|---|---|---|---|---|---|---|---|
D | A_deaminase | e1a4lD1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: A_deaminase | ECOD (1.6) |
A | A_deaminase | e1a4lA1 | 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 | e1a4lB1 | A: a/b barrels | X: TIM beta/alpha-barrel | H: TIM barrels (From Topology) | T: TIM barrels | F: A_deaminase | ECOD (1.6) |
C | A_deaminase | e1a4lC1 | 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) |
---|---|---|---|---|---|---|
D | 3.20.20.140 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Metal-dependent hydrolases | CATH (4.3.0) |
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) |
C | 3.20.20.140 | Alpha Beta | Alpha-Beta Barrel | TIM Barrel | Metal-dependent hydrolases | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR006330 | Adenosine/adenine deaminase | Family | |
IPR006650 | Adenosine/AMP deaminase active site | Active Site | |
IPR001365 | Adenosine deaminase domain | Domain | |
IPR032466 | Metal-dependent hydrolase | Homologous Superfamily | |
IPR028893 | Adenosine deaminase | Family |
Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage
Chains | Enzyme Name | Description | Catalytic 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] | EC: 3.5.4.4 (PDB Primary Data) |