› 5ifu

X-ray diffraction
2.45Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo tetramer
Assembly name:
PDBe Complex ID:
PDB-CPX-184694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Proline--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 506 amino acids
Theoretical weight: 58.99 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8I5R7 (Residues: 249-746; Coverage: 67%)
Gene names: PF3D7_1213800, PFL0670c, PRS, proRS
Sequence domains:

Ligands and Environments

4 bound ligands:
Ligand GBM 2 x GBM
Ligand CL 1 x CL
Ligand FMT 14 x FMT
Ligand EDO 2 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P43212
Unit cell:
a: 138.31Å b: 138.31Å c: 156.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.185 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Roles of aminoacyl-tRNA synthetases in immune regulation and immune diseases.
Nie et al. (2019)
2 more

4 mentions without citation

Biochemical and Structural Characterization of Selective Allosteric Inhibitors of the Plasmodium falciparum Drug Target, Prolyl-tRNA-synthetase.
Hewitt et al. (2017)
3 more