4a91

X-ray diffraction
1.75Å resolution

Crystal structure of the glutamyl-queuosine tRNAAsp synthetase from E. coli complexed with L-glutamate

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamyl-Q tRNA(Asp) synthetase Chain: A
Molecule details ›
Chain: A
Length: 298 amino acids
Theoretical weight: 33.64 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P27305 (Residues: 11-308; Coverage: 97%)
Gene names: JW5892, b0144, gluQ, yadB
Sequence domains: tRNA synthetases class I (E and Q), catalytic domain
Structure domains: HUPs

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2221
Unit cell:
a: 39.1Å b: 115.03Å c: 154.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.164 0.199
Expression system: Escherichia coli