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 Cited by PubMed: 11434768DOI: 10.1021/bi010641m PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
Download full validation report