› 1wkb

X-ray diffraction
2.05Å resolution

Crystal Structure of Leucyl-tRNA Synthetase from the Archaeon Pyrococcus horikoshii Reveals a Novel Editing Domain Orientation

Released:
DOI: 10.2210/pdb1wkb/pdb
PDB entry 1wkb coloured by chain, front view.
PDB entry 1wkb coloured by chain, side view.
PDB entry 1wkb coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Crystal structure of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii reveals a novel editing domain orientation.
Fukunaga R, Yokoyama S
J Mol Biol 346 57-71 (2005)
PMID: 15663927

Function and Biology Details

Reaction catalysed: 
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129754 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine--tRNA ligase Chain: A
Molecule details ›
Chain: A
Length: 810 amino acids
Theoretical weight: 95.64 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O58698 (Residues: 1-810; Coverage: 84%)
Gene names: PH0965, leuS
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand SO4 8 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: R3
Unit cell:
a: 186.196Å b: 186.196Å c: 91.428Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.18 0.218
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Aminoacyl-tRNA synthesis and translational quality control.
Ling et al. (2009)
5 more

9 mentions without citation

In silico discovery of aminoacyl-tRNA synthetase inhibitors.
Zhao et al. (2014)
8 more