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Structure paper

TitleThe deacylation mechanism of AmpC beta-lactamase at ultrahigh resolution
Journal, issue, pagesJ. Am. Chem. Soc., Vol. 128, Page 2970-2976, Year 2006
Publish dateDec 20, 2005 (structure data deposition date)
AuthorsChen, Y. / Minasov, G. / Roth, T.A. / Prati, F. / Shoichet, B.K.
External linksJ. Am. Chem. Soc. / PubMed:16506777
MethodsX-ray diffraction
Resolution1.07 Å
Structure data

PDB-2ffy:
AmpC beta-lactamase N289A mutant in complex with a boronic acid deacylation transition state analog compound SM3
Method: X-RAY DIFFRACTION / Resolution: 1.07 Å

Chemicals

ChemComp-K:
Unknown entry

ChemComp-SM3:
(1R)-1-(2-THIENYLACETYLAMINO)-1-PHENYLMETHYLBORONIC ACID

ChemComp-PO4:
PHOSPHATE ION

ChemComp-HOH:
WATER

Source
  • escherichia coli (E. coli)
KeywordsHYDROLASE / AmpC; beta-lactamase; deacylation; transition state; boronic acid

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