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Structure paper

TitleDoes targeting Arg98 of FimH lead to high affinity antagonists?
Journal, issue, pagesEur. J. Med. Chem., Vol. 211, Page 113093-113093, Year 2020
Publish dateNov 12, 2020 (structure data deposition date)
AuthorsTomasic, T. / Rabbani, S. / Jakob, R.P. / Reisner, A. / Jakopin, Z. / Maier, T. / Ernst, B. / Anderluh, M.
External linksEur. J. Med. Chem. / PubMed:33340913
MethodsX-ray diffraction
Resolution1.42 Å
Structure data

PDB-7ayn:
Crystal structure of the lectin domain of the FimH variant Arg98Ala, in complex with Methyl 3-chloro-4-D-mannopyranosyloxy-3-biphenylcarboxylate
Method: X-RAY DIFFRACTION / Resolution: 1.42 Å

Chemicals

ChemComp-SBQ:
methyl 3-[3-chloranyl-4-[(2~{R},3~{S},4~{S},5~{S},6~{R})-6-(hydroxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-phenyl]benzoate

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • escherichia coli k12 (bacteria)
KeywordsCELL ADHESION / adhesin / FimH / UPEC / bladder infection / carbohydrate / lectin

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