› 4hwt

X-ray diffraction
2.3Å resolution

Crystal structure of human Threonyl-tRNA synthetase bound to a novel inhibitor

Released:
DOI: 10.2210/pdb4hwt/pdb
PDB entry 4hwt coloured by chain, front view.
PDB entry 4hwt coloured by chain, side view.
PDB entry 4hwt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design.
Teng M, Hilgers MT, Cunningham ML, Borchardt A, Locke JB, Abraham S, Haley G, Kwan BP, Hall C, Hough GW, Shaw KJ, Finn J
J Med Chem 56 1748-60 (2013)
PMID: 23362938

Function and Biology Details

Reaction catalysed: 
ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150788 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Threonine--tRNA ligase 1, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 413 amino acids
Theoretical weight: 48.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P26639 (Residues: 321-723; Coverage: 56%)
Gene names: TARS, TARS1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand 1B2 2 x 1B2
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P41212
Unit cell:
a: 73.897Å b: 73.897Å c: 357.587Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.257
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

Evolutionary Limitation and Opportunities for Developing tRNA Synthetase Inhibitors with 5-Binding-Mode Classification.
Fang et al. (2015)
5 more

2 mentions without citation

Aminoacyl-tRNA Synthetases as Valuable Targets for Antimicrobial Drug Discovery.
Pang et al. (2021)
1 more