1ll5
From Proteopedia
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| - | [[Image:1ll5.gif|left|200px]] | + | [[Image:1ll5.gif|left|200px]] |
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| - | '''X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem''' | + | {{Structure |
| + | |PDB= 1ll5 |SIZE=350|CAPTION= <scene name='initialview01'>1ll5</scene>, resolution 1.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=IM2:3-(2-FORMIMIDOYLAMINO-ETHYLSULFANYL)-5-(1-FORMYL-2-HYDROXY-PROPYL)-4,5-DIHYDRO-1H-PYRROLE-2-CARBOXYLIC ACID'>IM2</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] | ||
| + | |GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''X-ray crystal structure of AmpC WT beta-lactamase in complex with covalently bound imipenem''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LL5 is a [ | + | 1LL5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LL5 OCA]. |
==Reference== | ==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:[http:// | + | Structural basis for imipenem inhibition of class C beta-lactamases., Beadle BM, Shoichet BK, Antimicrob Agents Chemother. 2002 Dec;46(12):3978-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12435704 12435704] |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: imipenem]] | [[Category: imipenem]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:32:07 2008'' |
Revision as of 10:32, 20 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | K12 (Escherichia coli) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| 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 Thu Mar 20 12:32:07 2008
