2ag6

X-ray diffraction
1.9Å resolution

Crystal structure of p-bromo-l-phenylalanine-tRNA sythetase in complex with p-bromo-l-phenylalanine

Released:
Primary publication:
Structural plasticity of an aminoacyl-tRNA synthetase active site.
Proc Natl Acad Sci U S A 103 6483-8 (2006)
PMID: 16618920

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 314 amino acids
Theoretical weight: 36.08 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q57834 (Residues: 1-306; Coverage: 100%)
Gene names: MJ0389, tyrS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P43212
Unit cell:
a: 102.719Å b: 102.719Å c: 70.598Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.247
Expression system: Escherichia coli BL21(DE3)