Function and Biology Details
Reaction catalysed:
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Threonine-tRNA ligase, class IIa
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Anticodon-binding
- Threonine-tRNA ligase, class IIa, anticodon-binding domain
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
- Aminoacyl-tRNA synthetase, class II
- Threonine-tRNA ligase catalytic core domain
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Threonine--tRNA ligase 1, cytoplasmic (preferred)
PDBe Complex ID:
PDB-CPX-150788 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase 1, cytoplasmic
Molecule details ›
Chains: A, B, C, D
Length: 415 amino acids
Theoretical weight: 48.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 415 amino acids
Theoretical weight: 48.47 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P26639 (Residues: 322-723; Coverage: 56%)
Sequence domains:
Structure domains:
