Function and Biology Details
Reaction catalysed:
ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Valine-tRNA ligase
- Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
- Rossmann-like alpha/beta/alpha sandwich fold
- Valyl-tRNA synthetase, tRNA-binding arm
- Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm
- Valyl-tRNA synthetase, tRNA-binding arm superfamily
- Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding
- Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
3 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Valine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-161204 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Valine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 862 amino acids
Theoretical weight: 98.91 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 862 amino acids
Theoretical weight: 98.91 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
- Canonical:
P96142 (Residues: 1-862; Coverage: 100%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL44XU
Spacegroup:
P21212
Expression system: Escherichia coli
