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TitleCrystal structure of AmpC BER and molecular docking lead to the discovery of broad inhibition activities of halisulfates against beta-lactamases.
Journal, issue, pagesComput Struct Biotechnol J, Vol. 19, Page 145-152, Year 2021
Publish dateJul 7, 2020 (structure data deposition date)
AuthorsJeong, B.G. / Na, J.H. / Bae, D.W. / Park, S.B. / Lee, H.S. / Cha, S.S.
External linksComput Struct Biotechnol J / PubMed:33425247
MethodsX-ray diffraction
Resolution1.79006366468 Å
Structure data

PDB-7cin:
Crystal structure of the extended-spectrum class C beta-lactamase AmpC BER with the ordered R2 loop
Method: X-RAY DIFFRACTION / Resolution: 1.79006366468 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli k-12 (bacteria)
KeywordsHYDROLASE / Class C beta-lactamase / wild-type AmpC BER / two amino acid insertion in the R2 loop / ordered R2 loop

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