Function and Biology Details
Reaction catalysed:
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Leucine-tRNA ligase
- Rossmann-like alpha/beta/alpha sandwich fold
- Aminoacyl-tRNA synthetase, class Ia
- Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding
- Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
- Leucyl-tRNA synthetase, domain 3
- Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
- Leucyl-tRNA synthetase, editing domain
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Leucine--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-181968 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Leucine--tRNA ligase
Molecule details ›
Chains: A, D
Length: 878 amino acids
Theoretical weight: 101.17 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Length: 878 amino acids
Theoretical weight: 101.17 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q7SIE4 (Residues: 1-878; Coverage: 100%)
Sequence domains:
- tRNA synthetases class I (M)
- Leucyl-tRNA synthetase, editing domain
- tRNA synthetases class I (I, L, M and V)
- Leucine-tRNA synthetase-specific domain
- Anticodon-binding domain of tRNA ligase
