Function and Biology Details
Reaction catalysed:
ATP + L-glutamate + tRNA(Glu) = AMP + diphosphate + L-glutamyl-tRNA(Glu)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glutamyl/glutaminyl-tRNA synthetase
- Glutamate-tRNA ligase, bacterial/mitochondrial
- Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2
- Aminoacyl-tRNA synthetase, class I, anticodon-binding
- Glutamate-tRNA synthetase, class I, anticodon-binding domain, subdomain 1
- Aminoacyl-tRNA synthetase, class I, anticodon-binding superfamily
- Aminoacyl-tRNA synthetase, class I, conserved site
- Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain
3 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Glutamate--tRNA ligase and RNA (preferred)
PDBe Complex ID:
PDB-CPX-150905 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Glutamate--tRNA ligase
Molecule details ›
Chains: A, C
Length: 468 amino acids
Theoretical weight: 53.98 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 468 amino acids
Theoretical weight: 53.98 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
- Canonical:
P27000 (Residues: 1-468; 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 BL-6A
Spacegroup:
C2221
Expression systems:
- Escherichia coli
- Not provided
