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Structure paper

TitleRefined crystal structure of beta-lactamase from Citrobacter freundii indicates a mechanism for beta-lactam hydrolysis.
Journal, issue, pagesNature, Vol. 343, Page 284-288, Year 1990
Publish dateSep 7, 2000 (structure data deposition date)
AuthorsOefner, C. / D'Arcy, A. / Daly, J.J. / Gubernator, K. / Charnas, R.L. / Heinze, I. / Hubschwerlen, C. / Winkler, F.K.
External linksNature / PubMed:2300174
MethodsX-ray diffraction
Resolution2 - 2.5 Å
Structure data

PDB-1fr1:
REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-1fr6:
REFINED CRYSTAL STRUCTURE OF BETA-LACTAMASE FROM CITROBACTER FREUNDII INDICATES A MECHANISM FOR BETA-LACTAM HYDROLYSIS
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-AZR:
2-({[(1Z)-1-(2-amino-1,3-thiazol-4-yl)-2-oxo-2-{[(2S,3S)-1-oxo-3-(sulfoamino)butan-2-yl]amino}ethylidene]amino}oxy)-2-methylpropanoic acid / antibiotic*YM

Source
  • citrobacter freundii (bacteria)
KeywordsHYDROLASE / Antibiotic Resistance / Class C Beta-lactamase / Monobactum

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