1wny

X-ray diffraction
1.6Å resolution

Isoleucyl-tRNA synthetase editing domain

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-isoleucine + tRNA(Ile) = AMP + diphosphate + L-isoleucyl-tRNA(Ile)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-157524 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Isoleucine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 20.63 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56690 (Residues: 200-385; Coverage: 18%)
Gene names: TTHA1067, ileS
Sequence domains: tRNA synthetases class I (I, L, M and V)
Structure domains: Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P41212
Unit cell:
a: 102.723Å b: 102.723Å c: 82.926Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.209
Expression system: Escherichia coli BL21(DE3)