CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.30 | 2-Layer Sandwich | |
3.30.1360 | Gyrase A; domain 2 | |
3.30.1360.30 | GAD-like domain |
Domain Context
CATH Clusters
Superfamily | GAD-like domain |
Functional Family |
Enzyme Information
6.1.1.23 |
Aspartate--tRNA(Asn) ligase.
based on mapping to UniProt A0QWN3
ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx).
-!- When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12. -!- It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). -!- This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon. -!- This accounts for the ability of this enzyme in, for example, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). -!- The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn).
|
UniProtKB Entries (1)
A0QWN3 |
SYDND_MYCS2
Mycolicibacterium smegmatis MC2 155
Aspartate--tRNA(Asp/Asn) ligase
|
PDB Structure
PDB | 4RMF |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Biochemical and Structural Characterization of Mycobacterial Aspartyl-tRNA Synthetase AspS, a Promising TB Drug Target.
Plos One
|