1o0c

X-ray diffraction
2.7Å resolution

CRYSTAL STRUCTURE OF L-GLUTAMATE AND AMPCPP BOUND TO GLUTAMINE AMINOACYL TRNA SYNTHETASE

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
Glutamine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 554 amino acids
Theoretical weight: 63.57 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A140NAB7 (Residues: 2-554; Coverage: 100%)
Gene names: ECBD_2981, glnS
Sequence domains: tRNA synthetases class I (E and Q), catalytic domain
Structure domains:
Glutaminyl tRNA Chain: B
Molecule details ›
Chain: B
Length: 75 nucleotides
Theoretical weight: 24.06 KDa
Source organism: Escherichia coli
Expression system: Not provided
Sequence domains: tRNA

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: C2221
Unit cell:
a: 241.1Å b: 94.58Å c: 116.08Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.215 0.213 0.265
Expression systems:
  • Escherichia coli
  • Not provided