1ll5 | pdb_00001ll5

X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem

spinqualitylabelsall models 1ll5, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ll5 is a 2 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IM2 Related: 1ke4, 1fco, 1bt5 Gene: K12 ("Bacillus coli" Migula 1895) Activity: Beta-lactamase, with EC number 3.5.2.6 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed To determine how imipenem inhibits the class C beta-lactamase AmpC, the X-ray crystal structure of the acyl-enzyme complex was determined to a resolution of 1.80 A. In the complex, the lactam carbonyl oxygen of imipenem has flipped by approximately 180 degrees compared to its expected position; the electrophilic acyl center is thus displaced from the point of hydrolytic attack. This conformation resembles that of imipenem bound to the class A enzyme TEM-1 but is different from that of moxalactam bound to AmpC. Structural basis for imipenem inhibition of class C beta-lactamases.,Beadle BM, Shoichet BK Antimicrob Agents Chemother. 2002 Dec;46(12):3978-80. PMID:12435704 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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