› 1jik

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-108016 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 420 amino acids
Theoretical weight: 47.66 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A6QHR2 (Residues: 1-420; Coverage: 100%)
Gene names: NWMN_1622, tyrS
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand 545 1 x 545
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: I212121
Unit cell:
a: 66.62Å b: 105.38Å c: 140.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.205 0.205 0.305
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Progress and challenges in aminoacyl-tRNA synthetase-based therapeutics.
Francklyn et al. (2019)
4 more

3 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
2 more