Function and Biology Details
Reaction catalysed:
ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Arginine-tRNA ligase
- Arginyl-tRNA synthetase, catalytic core domain
- Arginyl tRNA synthetase N-terminal domain
- Arginyl tRNA synthetase N-terminal domain superfamily
- DALR anticodon binding
- Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
- Aminoacyl-tRNA synthetase, class I, conserved site
- Rossmann-like alpha/beta/alpha sandwich fold
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Arginine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-188123 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine--tRNA ligase
Molecule details ›
Chain: A
Length: 592 amino acids
Theoretical weight: 66.32 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 592 amino acids
Theoretical weight: 66.32 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
- Canonical:
Q93RP5 (Residues: 1-592; Coverage: 100%)
Sequence domains:
- Arginyl tRNA synthetase N terminal domain
- tRNA synthetases class I (R)
- DALR anticodon binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
wwPDB Validation report is not available for this entry.
X-ray source:
SPRING-8 BEAMLINE BL41XU
Spacegroup:
P65
Expression system: Escherichia coli
