1I5Q

CRYSTAL STRUCTURE OF THE E. COLI AMPC BETA-LACTAMASE MUTANT N152A COVALENTLY ACYLATED WITH THE INHIBITORY BETA-LACTAM, MOXALACTAM

Summary for 1I5Q

• Entry DOI: 10.2210/pdb1i5q/pdb
• Related: 1FCO 2BLS
• Descriptor: BETA-LACTAMASE, (2R)-2-[(1R)-1-{[(2S)-2-carboxy-2-(4-hydroxyphenyl)acetyl]amino}-1-methoxy-2-oxoethyl]-5-methylidene-5,6-dihydro-2H-1,3-oxazine-4-carboxylic acid (3 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: 79902.48

Authors

Trehan, I.,Beadle, B.M.,Shoichet, B.K. (deposition date: 2001-02-28, release date: 2001-06-20, Last modification date: 2023-08-09)

• Primary citation: Trehan, I.,Beadle, B.M.,Shoichet, B.K.; Inhibition of AmpC beta-lactamase through a destabilizing interaction in the active site.; Biochemistry, 40:7992-7999, 2001; PubMed: 11434768; DOI: 10.1021/bi010641m

Experimental method

X-RAY DIFFRACTION (1.83 Å)