5vad

X-ray diffraction
2.36Å resolution

Crystal structure of human Prolyl-tRNA synthetase (PRS) in complex with inhibitor

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-139773 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bifunctional glutamate/proline--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 516 amino acids
Theoretical weight: 58.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P07814 (Residues: 998-1512; Coverage: 34%)
Gene names: EPRS, EPRS1, GLNS, PARS, PIG32, QARS, QPRS
Sequence domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: P21
Unit cell:
a: 71.089Å b: 92.278Å c: 84.832Å
α: 90° β: 111.18° γ: 90°
R-values:
R R work R free
0.199 0.196 0.262
Expression system: Escherichia coli