X-ray diffraction
1.75Å resolution

Structural basis for non-cognate amino acid discrimination by the valyl-tRNA synthetase editing domain


Function and Biology Details

Reaction catalysed:
ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Valine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.54 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P96142 (Residues: 193-337; Coverage: 17%)
Gene name: valS
Structure domains: Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P6522
Unit cell:
a: 95.49Å b: 95.49Å c: 72.3Å
α: 90° β: 90° γ: 120°
R R work R free
0.205 0.205 0.247
Expression system: Escherichia coli BL21(DE3)