› 6ilh

X-ray diffraction
2.5Å resolution

Crystal Structure of human lysyl-tRNA synthetase L350H mutant

Released:
DOI: 10.2210/pdb6ilh/pdb
PDB 6ilh coloured by chain and viewed from the front.
PDB 6ilh coloured by chain and viewed from the side.
PDB 6ilh coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Retractile lysyl-tRNA synthetase-AIMP2 assembly in the human multi-aminoacyl-tRNA synthetase complex.
Hei Z, Wu S, Liu Z, Wang J, Fang P
J Biol Chem 294 4775-4783 (2019)
PMID: 30733335

Function and Biology Details

Reaction catalysed: 
ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lysine--tRNA ligase Chains: A, B
Molecule details ›
Chains: A, B
Length: 521 amino acids
Theoretical weight: 60.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q15046 (Residues: 70-581; Coverage: 86%)
Gene names: KARS, KARS1, KIAA0070
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand KAA 2 x KAA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U1
Spacegroup: P3221
Unit cell:
a: 152.18Å b: 152.18Å c: 106.32Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.194 0.226
Expression system: Escherichia coli

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Citations

3 review citations

Aminoacyl-tRNA synthetases of the multi-tRNA synthetase complex and their role in tumorigenesis.
Khan et al. (2022)
2 more