› 1r6t

X-ray diffraction
2.1Å resolution

crystal structure of human tryptophanyl-tRNA synthetase

Released:
DOI: 10.2210/pdb1r6t/pdb
PDB entry 1r6t coloured by chain, front view.
PDB entry 1r6t coloured by chain, side view.
PDB entry 1r6t coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains.
Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L
Proc Natl Acad Sci U S A 100 15376-80 (2003)
PMID: 14671330

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 domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tryptophan--tRNA ligase, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 477 amino acids
Theoretical weight: 54.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23381 (Residues: 1-466; Coverage: 99%)
Gene names: IFI53, WARS, WARS1, WRS
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand TYM 1 x TYM
Ligand GOL 2 x GOL
1 modified residue:
Ligand MSE 24 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2
Unit cell:
a: 152.146Å b: 95.713Å c: 98.506Å
α: 90° β: 91.62° γ: 90°
R-values:
R R work R free
0.208 0.208 0.239
Expression system: Escherichia coli

Quick links

Citations

5 review citations

New functions of aminoacyl-tRNA synthetases beyond translation.
Guo et al. (2010)
4 more

23 mentions without citation

Neurodegenerative Charcot-Marie-Tooth disease as a case study to decipher novel functions of aminoacyl-tRNA synthetases.
Wei et al. (2019)
22 more