› 2quj

X-ray diffraction
2.42Å resolution

Crystal structures of human tryptophanyl-tRNA synthetase in complex with TrpAMP

Released:
DOI: 10.2210/pdb2quj/pdb
PDB entry 2quj coloured by chain, front view.
PDB entry 2quj coloured by chain, side view.
PDB entry 2quj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic mechanism of the tryptophan activation reaction revealed by crystal structures of human tryptophanyl-tRNA synthetase in different enzymatic states.
Shen N, Zhou M, Yang B, Yu Y, Dong X, Ding J
Nucleic Acids Res 36 1288-99 (2008)
PMID: 18180246

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-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: 54.06 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23381 (Residues: 1-471; Coverage: 100%)
Gene names: IFI53, WARS, WARS1, WRS
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand CL 9 x CL
Ligand TYM 1 x TYM
Ligand GOL 4 x GOL
Ligand TRP 1 x TRP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P422
Unit cell:
a: 80Å b: 80Å c: 383Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.214 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Adenylate-forming enzymes.
Schmelz et al. (2009)
2 more

6 mentions without citation

Crystal structure of a mammalian CTP: phosphocholine cytidylyltransferase catalytic domain reveals novel active site residues within a highly conserved nucleotidyltransferase fold.
Lee et al. (2009)
5 more