Function and Biology Details
Reaction catalysed:
ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Aspartyl/Asparaginyl-tRNA synthetase, class IIb
- Aspartate-tRNA synthetase, type 2
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Nucleic acid-binding, OB-fold
- Aminoacyl-tRNA synthetase, class II
- Aminoacyl-tRNA synthetase, class II (D/K/N)
- OB-fold nucleic acid binding domain, AA-tRNA synthetase-type
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Aspartate--tRNA(Asp) ligase (preferred)
PDBe Complex ID:
PDB-CPX-176006 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate--tRNA(Asp) ligase
Molecule details ›
Chains: A, B
Length: 438 amino acids
Theoretical weight: 50.98 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 438 amino acids
Theoretical weight: 50.98 KDa
Source organism: Thermococcus kodakarensis KOD1
Expression system: Escherichia coli
UniProt:
- Canonical:
Q52428 (Residues: 1-438; Coverage: 100%)
Sequence domains:
Structure domains:
