X-ray diffraction
2.28Å resolution

Crystal Structure of Prolyl-tRNA synthetase (ProRS, Proline-tRNA ligase) from Plasmodium falciparum in complex with MAT334 and L-Proline

Source organism: Plasmodium falciparum 3D7
Entry authors: Johansson C, Tye M, Payne NC, Mazitschek R, Oppermann UCT

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Proline--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 504 amino acids
Theoretical weight: 58.53 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
  • Canonical: Q8I5R7 (Residues: 249-746; Coverage: 67%)
Gene names: PF3D7_1213800, PFL0670c, PRS, proRS
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P3221
Unit cell:
a: 103.5Å b: 103.5Å c: 127.51Å
α: 90° β: 90° γ: 120°
R R work R free
0.229 0.228 0.253
Expression system: Escherichia coli BL21(DE3)