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TitleBinding of cephalothin and cefotaxime to D-ala-D-ala-peptidase reveals a functional basis of a natural mutation in a low-affinity penicillin-binding protein and in extended-spectrum beta-lactamases.
Journal, issue, pagesBiochemistry, Vol. 34, Page 9532-9540, Year 1995
Publish dateJan 12, 1995 (structure data deposition date)
AuthorsKuzin, A.P. / Liu, H. / Kelly, J.A. / Knox, J.R.
External linksBiochemistry / PubMed:7626623
MethodsX-ray diffraction
Resolution1.8 - 2.04 Å
Structure data

PDB-1cef:
CEFOTAXIME COMPLEXED WITH THE STREPTOMYCES R61 DD-PEPTIDASE
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

PDB-1ceg:
CEPHALOTHIN COMPLEXED WITH DD-PEPTIDASE
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-CEF:
CEFOTAXIME, C3' cleaved, open, bound form / antibiotic*YM

ChemComp-HOH:
WATER

ChemComp-CEP:
CEPHALOTHIN GROUP

Source
  • streptomyces sp. (bacteria)
KeywordsHYDROLASE-TRANSPEPTIDASE / D-AMINO ACID PEPTIDASE / PENICILLIN TARGET

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