4zya

X-ray diffraction
1.65Å resolution

The N-terminal extension domain of human asparaginyl-tRNA synthetase

Released:

Function and Biology Details

Reaction catalysed:
ATP + L-asparagine + tRNA(Asn) = AMP + diphosphate + L-asparaginyl-tRNA(Asn)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-129107 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Asparagine--tRNA ligase, cytoplasmic Chains: A, B
Molecule details ›
Chains: A, B
Length: 77 amino acids
Theoretical weight: 9.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43776 (Residues: 4-77; Coverage: 14%)
Gene names: NARS, NARS1, NRS
Sequence domains: Asparaginal-tRNA synthetase, N-terminal domain
Structure domains: asparaginyl-tRNA synthetase, N-terminal domain

Ligands and Environments

3 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 7A (6B, 6C1)
Spacegroup: P65
Unit cell:
a: 32.626Å b: 32.626Å c: 215.921Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.206 0.254
Expression system: Escherichia coli