Structure analysis

N-terminal editing domain of threonyl-tRNA synthetase from Aeropyrum pernix with L-Ser3AA (snapshot 1)

X-ray diffraction
1.88Å resolution
Source organism: Aeropyrum pernix K1
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 11458.68 Å2
Buried surface area: 3635.33 Å2
Dissociation area: 1,065.25 Å2
Dissociation energy (ΔGdiss): 2.67 kcal/mol
Dissociation entropy (TΔSdiss): 11.82 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-195497

Macromolecules

Chain: A
Length: 136 amino acids
Theoretical weight: 15.14 KDa
Source organism: Aeropyrum pernix K1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9YFY3 (Residues: 1-136; Coverage: 32%)
Gene names: APE_0117.1, thrS2
Pfam: Archaea-specific editing domain of threonyl-tRNA synthetase
InterPro:
CATH: D-tyrosyl-tRNA(Tyr) deacylase

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