1FSY

AMPC BETA-LACTAMASE FROM E. COLI COMPLEXED WITH INHIBITOR CLOXACILLINBORONIC ACID

Summary for 1FSY

• Entry DOI: 10.2210/pdb1fsy/pdb
• Related: 1C3B 1FSW 2BLS 3BLS
• Descriptor: CEPHALOSPORINASE, PHOSPHATE ION, N-[5-METHYL-3-O-TOLYL-ISOXAZOLE-4-CARBOXYLIC ACID AMIDE] BORONIC ACID, ... (4 entities in total)
• Functional Keywords: cephalosporinase, beta-lactamase, serine hydrolase, hydrolase
• Biological source: Escherichia coli
• Cellular location: Periplasm: P00811
• Total number of polymer chains: 2
• Total formula weight: 79745.71

Authors

Caselli, E.,Powers, R.A.,Blasczcak, L.C.,Wu, C.Y.,Prati, F.,Shoichet, B.K. (deposition date: 2000-09-11, release date: 2001-03-14, Last modification date: 2024-10-30)

Primary citation

Caselli, E.,Powers, R.A.,Blasczcak, L.C.,Wu, C.Y.,Prati, F.,Shoichet, B.K.
Energetic, structural, and antimicrobial analyses of beta-lactam side chain recognition by beta-lactamases.
Chem.Biol., 8:17-31, 2001

PubMed Abstract: Penicillins and cephalosporins are among the most widely used and successful antibiotics. The emergence of resistance to these beta-lactams, most often through bacterial expression of beta-lactamases, threatens public health. To understand how beta-lactamases recognize their substrates, it would be helpful to know their binding energies. Unfortunately, these have been difficult to measure because beta-lactams form covalent adducts with beta-lactamases. This has complicated functional analyses and inhibitor design.

PubMed: 11182316
DOI: 10.1016/S1074-5521(00)00052-1

Experimental method

X-RAY DIFFRACTION (1.75 Å)