Function and Biology Details
Reaction catalysed:
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- WHEP-TRS domain
- 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)
- Aminoacyl-tRNA synthetase, class II
- Glycyl-tRNA synthetase-like core domain
- Glycyl-tRNA synthetase
2 more domains
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Glycine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-154355 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine--tRNA ligase
Molecule details ›
Chain: A
Length: 693 amino acids
Theoretical weight: 78.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 693 amino acids
Theoretical weight: 78.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P41250 (Residues: 55-739; Coverage: 93%)
Sequence domains:
Structure domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRL BEAMLINE BL11-1
Spacegroup:
P43212
Expression system: Escherichia coli BL21(DE3)
