X-ray diffraction
2.22Å resolution

2.2 Angstrom Crystal Structure of a Human Arginyl-tRNA Synthetase

Source organism: Homo sapiens
Entry authors: Smith AT, Rosenzweig AC

Function and Biology Details

Reaction catalysed:
ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Arginine--tRNA ligase, cytoplasmic Chain: A
Molecule details ›
Chain: A
Length: 601 amino acids
Theoretical weight: 68.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: P54136 (Residues: 73-660; Coverage: 89%)
Gene names: RARS, RARS1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 54.72Å b: 61.92Å c: 208.47Å
α: 90° β: 90° γ: 90°
R R work R free
0.221 0.219 0.264
Expression system: Escherichia coli