› 4p71

X-ray diffraction
2.79Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191226 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phenylalanine--tRNA ligase beta subunit Chains: A, B
Molecule details ›
Chains: A, B
Length: 792 amino acids
Theoretical weight: 86.9 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I0A4 (Residues: 1-792; Coverage: 100%)
Gene names: PA2739, pheT
Sequence domains:
Structure domains:
Phenylalanine--tRNA ligase alpha subunit Chains: C, D
Molecule details ›
Chains: C, D
Length: 338 amino acids
Theoretical weight: 38.11 KDa
Source organism: Pseudomonas aeruginosa PAO1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9I0A3 (Residues: 1-338; Coverage: 100%)
Gene names: PA2740, pheS
Sequence domains:
Structure domains: Bira Bifunctional Protein; Domain 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2
Unit cell:
a: 112.78Å b: 219.08Å c: 107.13Å
α: 90° β: 101.91° γ: 90°
R-values:
R R work R free
0.193 0.191 0.227
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Aminoacyl-tRNA synthetases.
Rubio Gomez et al. (2020)
2 more

3 mentions without citation

The role of a novel auxiliary pocket in bacterial phenylalanyl-tRNA synthetase druggability.
Abibi et al. (2014)
2 more