Function and Biology Details
Reaction catalysed:
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Class II Aminoacyl-tRNA synthetase/Biotinyl protein ligase (BPL) and lipoyl protein ligase (LPL)
- Anticodon-binding
- Anticodon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class II (G/ P/ S/T)
- Glycyl-tRNA synthetase-like core domain
- Glycyl-tRNA synthetase/DNA polymerase subunit gamma-2
- Aminoacyl-tRNA synthetase, class II
- Glycyl-tRNA synthetase
1 more domain
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
Glycine--tRNA ligase and peptide (preferred)
PDBe Complex ID:
PDB-CPX-157422 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Glycine--tRNA ligase
Molecule details ›
Chains: A, B
Length: 505 amino acids
Theoretical weight: 58.16 KDa
Source organism: Thermus thermophilus HB8
UniProt:
Sequence domains:
Structure domains:
Length: 505 amino acids
Theoretical weight: 58.16 KDa
Source organism: Thermus thermophilus HB8
UniProt:
- Canonical:
P56206 (Residues: 3-506; Coverage: 100%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
LURE BEAMLINE DW32, EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup:
C2221
