Function and Biology Details
Reaction catalysed:
ATP + L-serine + tRNA(Sec) = AMP + diphosphate + L-seryl-tRNA(Sec)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Serine-tRNA ligase, type1
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
- Aminoacyl-tRNA synthetase, class II
- Serine-tRNA ligase catalytic core domain
- Serine-tRNA synthetase, type1, N-terminal domain superfamily
- Serine-tRNA synthetase, type1, N-terminal
- Class I and II aminoacyl-tRNA synthetase, tRNA-binding arm
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Serine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-129727 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 53.34 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 455 amino acids
Theoretical weight: 53.34 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
- Canonical:
O58441 (Residues: 1-455; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup:
P212121
Expression system: Escherichia coli
