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Crystal structure of the aminoacylation catalytic fragment of human tryptophanyl-tRNA synthetase

X-ray diffraction
2.5Å resolution
PDB entry 1o5t coloured by chain, front view.
PDB entry 1o5t coloured by chain, side view.
PDB entry 1o5t coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: T2-TrpRS
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Multimeric state: homo dimer
Accessible surface area: 31463.81 Å2
Buried surface area: 3029.34 Å2
Dissociation area: 1,514.67 Å2
Dissociation energy (ΔGdiss): 18.38 kcal/mol
Dissociation entropy (TΔSdiss): 14.1 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-149944

Macromolecules

T2-TrpRS
Chain: A
Length: 378 amino acids
Theoretical weight: 43.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23381 (Residues: 94-471; Coverage: 80%)
Gene names: IFI53, WARS, WARS1, WRS
Pfam: tRNA synthetases class I (W and Y)
InterPro:
CATH:
SCOP: Class I aminoacyl-tRNA synthetases (RS), catalytic domain
T2-TrpRS in PDB entry 1o5t, assembly 1, front view.
T2-TrpRS in PDB entry 1o5t, assembly 1, side view.
T2-TrpRS in PDB entry 1o5t, assembly 1, top view.
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