› 1d2r

X-ray diffraction
2.9Å resolution

2.9 A CRYSTAL STRUCTURE OF LIGAND-FREE TRYPTOPHANYL-TRNA SYNTHETASE: DOMAIN MOVEMENTS FRAGMENT THE ADENINE NUCLEOTIDE BINDING SITE.

Released:
DOI: 10.2210/pdb1d2r/pdb
PDB entry 1d2r coloured by chain, front view.
PDB entry 1d2r coloured by chain, side view.
PDB entry 1d2r coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
2.9 A crystal structure of ligand-free tryptophanyl-tRNA synthetase: domain movements fragment the adenine nucleotide binding site.
Ilyin VA, Temple B, Hu M, Li G, Yin Y, Vachette P, Carter CW
Protein Sci 9 218-31 (2000)
PMID: 10716174

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 domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133715 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 326 amino acids
Theoretical weight: 36.75 KDa
Source organism: Geobacillus stearothermophilus
UniProt:
  • Canonical: P00953 (Residues: 1-326; Coverage: 99%)
Gene name: trpS
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: C2
Unit cell:
a: 226.76Å b: 91.66Å c: 156.97Å
α: 90° β: 132.66° γ: 90°
R-values:
R R work R free
0.237 0.237 0.262

Quick links

Citations

8 review citations

tRNA synthetase: tRNA aminoacylation and beyond.
Pang et al. (2014)
7 more

10 mentions without citation

Overview of protein structural and functional folds.
Sun et al. (2004)
9 more