Function and Biology Details
Reaction catalysed:
ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx)
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/Asn) ligase (preferred)
PDBe Complex ID:
PDB-CPX-177949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate--tRNA(Asp/Asn) ligase
Molecule details ›
Chains: A, B
Length: 422 amino acids
Theoretical weight: 48.4 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 422 amino acids
Theoretical weight: 48.4 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q5SIC2 (Residues: 1-422; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-4
Spacegroup:
P212121
Expression system: Escherichia coli
