1n3l

X-ray diffraction
1.18Å resolution

Crystal structure of a human aminoacyl-tRNA synthetase cytokine

Released:
Source organism: Homo sapiens
Primary publication:
Crystal structure of a human aminoacyl-tRNA synthetase cytokine.
Proc. Natl. Acad. Sci. U.S.A. 99 15369-74 (2002)
PMID: 12427973

Function and Biology Details

Reaction catalysed:
ATP + L-tyrosine + tRNA(Tyr) = AMP + diphosphate + L-tyrosyl-tRNA(Tyr)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Tyrosine--tRNA ligase, cytoplasmic, N-terminally processed Chain: A
Molecule details ›
Chain: A
Length: 372 amino acids
Theoretical weight: 42.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P54577 (Residues: 1-364; Coverage: 69%)
Gene names: YARS, YARS1
Sequence domains: tRNA synthetases class I (W and Y)
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P21212
Unit cell:
a: 74.595Å b: 162.392Å c: 35.603Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.223
Expression system: Escherichia coli