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Structure paper

TitleRole of the Hydrophobic Bridge in the Carbapenemase Activity of Class D beta-Lactamases.
Journal, issue, pagesAntimicrob. Agents Chemother., Vol. 63, Year 2019
Publish dateNov 27, 2018 (structure data deposition date)
AuthorsStewart, N.K. / Smith, C.A. / Antunes, N.T. / Toth, M. / Vakulenko, S.B.
External linksAntimicrob. Agents Chemother. / PubMed:30530607
MethodsX-ray diffraction
Resolution1.25 - 3.501 Å
Structure data

PDB-6n6t:
OXA-23 mutant F110A/M221A low pH form
Method: X-RAY DIFFRACTION / Resolution: 1.25 Å

PDB-6n6u:
OXA-23 mutant F110A/M221A low pH form imipenem complex
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-6n6v:
OXA-23 mutant F110A/M221A low pH form meropenem complex
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-6n6w:
OXA-23 mutant F110A/M221A neutral pH form
Method: X-RAY DIFFRACTION / Resolution: 3.25 Å

PDB-6n6x:
OXA-23 mutant F110A/M221A neutral pH form imipenem complex
Method: X-RAY DIFFRACTION / Resolution: 3.1 Å

PDB-6n6y:
OXA-23 mutant F110A/M221A neutral pH form meropenem complex
Method: X-RAY DIFFRACTION / Resolution: 3.501 Å

Chemicals

ChemComp-FLC:
CITRATE ANION

ChemComp-HOH:
WATER

ChemComp-ID1:
Imipenem / antibiotic*YM

ChemComp-KE1:
meropenem, bound form

ChemComp-SO4:
SULFATE ION

Source
  • acinetobacter baumannii (bacteria)
KeywordsHYDROLASE / carbapenemase / antibiotic resistance / mutant

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