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
- GAD-like domain superfamily
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Aspartate-tRNA ligase, type 1
- Nucleic acid-binding, OB-fold
- GAD domain
- Aspartate-tRNA ligase, type 1, core domain
- Aminoacyl-tRNA synthetase, class II
3 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Aspartate--tRNA ligase, mitochondrial (preferred)
PDBe Complex ID:
PDB-CPX-180164 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Aspartate--tRNA ligase, mitochondrial
Molecule details ›
Chains: A, B, C, D
Length: 617 amino acids
Theoretical weight: 70.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains:
Structure domains:
Length: 617 amino acids
Theoretical weight: 70.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q6PI48 (Residues: 41-645; Coverage: 94%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SLS BEAMLINE X10SA
Spacegroup:
P2
Expression system: Escherichia coli BL21
