1ll5
From Proteopedia
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| , resolution 1.80Å | |||||||
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| Ligands: | |||||||
| Gene: | K12 (Escherichia coli) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Related: | 1KE4, 1FCO, 1BT5
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem
Overview
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.
About this Structure
1LL5 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Sun Mar 30 22:04:09 2008
