4q15

X-ray diffraction
2.35Å resolution

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline--tRNA ligase) from Plasmodium falciparum in complex with Halofuginone and AMPPNP in space group P212121 at 2.35 A

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
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
UniProt:
  • Canonical: Q8I5R7 (Residues: 249-746; Coverage: 67%)
Gene names: PF3D7_1213800, PFL0670c, PRS, proRS
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P212121
Unit cell:
a: 76.58Å b: 78.09Å c: 167.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.219
Expression system: Escherichia coli