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Structure paper

TitleSeryl-tRNA synthetase from Escherichia coli,implication of its N-terminal domain in aminoacylation activity and specificity.
Journal, issue, pagesNucleic Acids Res, Vol. 22, Page 2963-2969, Year 1994
Publish dateMar 26, 2025 (structure data deposition date)
AuthorsBorel, F. / Vincent, C. / Leberman, R. / Hartlein, M.
External linksNucleic Acids Res / PubMed:8065908
MethodsX-ray diffraction
Resolution2.32 Å
Structure data

PDB-9qof:
E.coli seryl-tRNA synthetase (Arm deletion mutant) bound to sulphamoyl seryl-adenylate analogue
Method: X-RAY DIFFRACTION / Resolution: 2.32 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-SO4:
SULFATE ION

ChemComp-SSA:
5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
KeywordsTRANSLATION / aminoacyl-tRNA synthetase / ATP binding

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