› 2o5r

X-ray diffraction
2.34Å resolution

Crystal structure of Glutamyl-tRNA synthetase 1 (EC 6.1.1.17) (Glutamate-tRNA ligase 1) (GluRS 1) (TM1351) from Thermotoga maritima at 2.5 A resolution

Released:
DOI: 10.2210/pdb2o5r/pdb
PDB entry 2o5r coloured by chain, front view.
PDB entry 2o5r coloured by chain, side view.
PDB entry 2o5r coloured by chain, top view.
Source organism: Thermotoga maritima
Entry author: Joint Center for Structural Genomics (JCSG)

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:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194767 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutamate--tRNA ligase 1 Chain: A
Molecule details ›
Chain: A
Length: 481 amino acids
Theoretical weight: 56.85 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X172 (Residues: 1-469; Coverage: 100%)
Gene names: TM_1351, gltX1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CL 3 x CL
Ligand GOL 1 x GOL
1 modified residue:
Ligand MSE 15 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3121
Unit cell:
a: 69.953Å b: 69.953Å c: 283.945Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.234 0.268
Expression system: Escherichia coli

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