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TitleBurkholderia pseudomallei PenI beta-lactamase and variants are potently inhibited by taniborbactam.
Journal, issue, pagesAntimicrob. Agents Chemother., Vol. 69, Page e0078725-e0078725, Year 2025
Publish dateSep 30, 2024 (structure data deposition date)
AuthorsMojica, M.F. / Becka, S.A. / Edwards, M. / Myers, C. / Uehara, K. / Uehara, T. / Hoshino, T. / Zeiser, E.T. / Chatwin, C.L. / Six, D.A. ...Mojica, M.F. / Becka, S.A. / Edwards, M. / Myers, C. / Uehara, K. / Uehara, T. / Hoshino, T. / Zeiser, E.T. / Chatwin, C.L. / Six, D.A. / Bonomo, R.A. / Papp-Wallace, K.M. / Nukaga, M.
External linksAntimicrob. Agents Chemother. / PubMed:40938351
MethodsX-ray diffraction
Resolution1.25 Å
Structure data

PDB-9jse:
Crystal Structure of PenI beta-Lactamase from Burkholderia pseudomallei Complex with Taniborbactam
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

Chemicals

ChemComp-KJK:
(3~{R})-3-[2-[4-(2-azanylethylamino)cyclohexyl]ethanoylamino]-2-oxidanyl-3,4-dihydro-1,2-benzoxaborinine-8-carboxylic acid

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • burkholderia pseudomallei k96243 (bacteria)
KeywordsHYDROLASE / beta-lactamase

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