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, cytoplasmic (preferred)
PDBe Complex ID:
PDB-CPX-156949 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Arginine--tRNA ligase, cytoplasmic
Molecule details ›
Chain: A
Length: 601 amino acids
Theoretical weight: 68.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 601 amino acids
Theoretical weight: 68.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P54136 (Residues: 73-660; Coverage: 89%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 21-ID-G
Spacegroup:
P212121
Expression system: Escherichia coli
