Function and Biology Details
Reaction catalysed:
ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Isoleucine-tRNA ligase
- Rossmann-like alpha/beta/alpha sandwich fold
- Zinc finger, FPG/IleRS-type
- Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase, anticodon-binding
- Aminoacyl-tRNA synthetase, class Ia, anticodon-binding
- Isoleucyl tRNA synthetase type 1, anticodon-binding domain
- Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain
- Aminoacyl-tRNA synthetase, class I, conserved site
3 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Isoleucine--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-154474 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Isoleucine--tRNA ligase
Molecule details ›
Chain: A
Length: 917 amino acids
Theoretical weight: 105.06 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 917 amino acids
Theoretical weight: 105.06 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
- Canonical:
P41972 (Residues: 1-917; Coverage: 100%)
Sequence domains:
- tRNA synthetases class I (I, L, M and V)
- Anticodon-binding domain of tRNA ligase
- Zinc finger found in FPG and IleRS
