› 2a4m

X-ray diffraction
2.3Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193298 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 331 amino acids
Theoretical weight: 36.13 KDa
Source organism: Deinococcus radiodurans
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9RVD6 (Residues: 21-351; Coverage: 94%)
Gene names: DR_1093, trpS2, trpSII
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand TRP 1 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: C2
Unit cell:
a: 212.582Å b: 58.574Å c: 85.15Å
α: 90° β: 96.64° γ: 90°
R-values:
R R work R free
0.24 0.23 0.27
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Bacterial nitric oxide synthases.
Crane et al. (2010)
1 more

1 mention without citation

An appended domain results in an unusual architecture for malaria parasite tryptophanyl-tRNA synthetase.
Khan et al. (2013)