› 1ulh

X-ray diffraction
2.31Å resolution

A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase

Released:
DOI: 10.2210/pdb1ulh/pdb
PDB entry 1ulh coloured by chain, front view.
PDB entry 1ulh coloured by chain, side view.
PDB entry 1ulh coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A short peptide insertion crucial for angiostatic activity of human tryptophanyl-tRNA synthetase.
Kise Y, Lee SW, Park SG, Fukai S, Sengoku T, Ishii R, Yokoyama S, Kim S, Nureki O
Nat Struct Mol Biol 11 149-56 (2004)
PMID: 14730354

Function and Biology Details

Reaction catalysed: 
ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophyl-tRNA(Trp)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
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:
T1-TrpRS Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 44.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P23381 (Residues: 82-471; Coverage: 83%)
Gene names: IFI53, WARS, WARS1, WRS
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: SPRING-8 BEAMLINE BL41XU
Spacegroup: C2
Unit cell:
a: 136.025Å b: 96.606Å c: 98.319Å
α: 90° β: 130.26° γ: 90°
R-values:
R R work R free
0.275 0.241 0.292
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

12 review citations

Aminoacyl tRNA synthetases and their connections to disease.
Park et al. (2008)
11 more

6 mentions without citation

Functional and crystal structure analysis of active site adaptations of a potent anti-angiogenic human tRNA synthetase.
Yang et al. (2007)
5 more