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:
hetero tetramer (preferred)
Assembly name:
Threonine--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-141714 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Threonine--tRNA ligase
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 401 amino acids
Theoretical weight: 46.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 401 amino acids
Theoretical weight: 46.73 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A8M3 (Residues: 242-642; Coverage: 63%)
Sequence domains:
Structure domains:
