Function and Biology Details
Reaction catalysed:
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Threonine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-194140 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 16.28 KDa
Source organism: Pyrococcus abyssi
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Archaea-specific editing domain of threonyl-tRNA synthetase
Structure domains: D-tyrosyl-tRNA(Tyr) deacylase
Length: 143 amino acids
Theoretical weight: 16.28 KDa
Source organism: Pyrococcus abyssi
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9UZ14 (Residues: 1-143; Coverage: 23%)
Sequence domains: Archaea-specific editing domain of threonyl-tRNA synthetase
Structure domains: D-tyrosyl-tRNA(Tyr) deacylase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU RU300
Spacegroup:
P3221
Expression system: Escherichia coli BL21(DE3)
