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Structure paper

TitleSidF, a dual substrate N5-acetyl-N5-hydroxy-L-ornithine transacetylase involved in Aspergillus fumigatus siderophore biosynthesis.
Journal, issue, pagesJ Struct Biol X, Vol. 11, Page 100119-100119, Year 2025
Publish dateDec 3, 2021 (structure data deposition date)
AuthorsPoonsiri, T. / Stransky, J. / Demitri, N. / Haas, H. / Cianci, M. / Benini, S.
External linksJ Struct Biol X / PubMed:39845173
MethodsX-ray diffraction
Resolution1.87 - 2.581 Å
Structure data

PDB-7qf6:
N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF
Method: X-RAY DIFFRACTION / Resolution: 1.87 Å

PDB-8kd8:
N(5)-hydroxyornithine:cis-anhydromevalonyl coenzyme A-N(5)-transacylase sidF N-terminal domain
Method: X-RAY DIFFRACTION / Resolution: 2.581 Å

Chemicals

ChemComp-GOL:
GLYCEROL

ChemComp-SCN:
THIOCYANATE ION

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

Source
  • aspergillus fumigatus (mold)
  • aspergillus fumigatus (strain atcc mya-4609 / cbs 101355 / fgsc a1100 / af293) (mold)
KeywordsTRANSFERASE / Hydroxyornithine transacylase / GNAT / SidF / Aspergillus fumigatus / siderophore / acetyltransferase

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