Function and Biology Details
Reaction catalysed:
ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Glutamyl/glutaminyl-tRNA synthetase
- Large ribosomal subunit protein bL25/Gln-tRNA synthetase, N-terminal
- Glutamyl/glutaminyl-tRNA synthetase, class Ib, anti-codon binding domain
- Large ribosomal subunit protein bL25/Gln-tRNA synthetase, anti-codon-binding domain superfamily
- Aminoacyl-tRNA synthetase, class I, conserved site
- Glutamine-tRNA synthetase
- Glutamyl/glutaminyl-tRNA synthetase, class Ib, catalytic domain
- Rossmann-like alpha/beta/alpha sandwich fold
4 more domains
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Glutamine--tRNA ligase (preferred)
PDBe Complex ID:
PDB-CPX-155672 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamine--tRNA ligase
Molecule details ›
Chain: A
Length: 776 amino acids
Theoretical weight: 88.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 776 amino acids
Theoretical weight: 88.1 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P47897 (Residues: 1-775; Coverage: 100%)
Sequence domains:
- Glutaminyl-tRNA synthetase, non-specific RNA binding region part 1
- Glutaminyl-tRNA synthetase, non-specific RNA binding region part 2
- tRNA synthetases class I (E and Q), catalytic domain
- tRNA synthetases class I (E and Q), anti-codon binding domain
- tRNA synthetases class I (E and Q), anti-codon binding domain
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 23-ID-D
Spacegroup:
P21212
Expression system: Escherichia coli
