3o0a

X-ray diffraction
1.77Å resolution

Crystal structure of the wild type CP1 hydrolitic domain from Aquifex Aeolicus leucyl-trna

Released:
Source organism: Aquifex aeolicus
Entry authors: Cura V, Olieric N, Wang E-D, Moras D, Eriani G, Cavarelli J

Function and Biology Details

Reaction catalysed:
ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-tRNA(Leu)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-130365 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine--tRNA ligase subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 24.89 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O66680 (Residues: 225-443; Coverage: 35%)
Gene names: aq_351, leuS
Sequence domains: Leucyl-tRNA synthetase, editing domain
Structure domains: Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 38.689Å b: 98.18Å c: 116.667Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.225
Expression system: Escherichia coli