1ll5
From Proteopedia
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|PDB= 1ll5 |SIZE=350|CAPTION= <scene name='initialview01'>1ll5</scene>, resolution 1.80Å | |PDB= 1ll5 |SIZE=350|CAPTION= <scene name='initialview01'>1ll5</scene>, resolution 1.80Å | ||
|SITE= | |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> | + | |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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= K12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ke4|1KE4]], [[1fco|1FCO]], [[1bt5|1BT5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ll5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ll5 OCA], [http://www.ebi.ac.uk/pdbsum/1ll5 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ll5 RCSB]</span> | ||
}} | }} | ||
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[[Category: Beadle, B M.]] | [[Category: Beadle, B M.]] | ||
[[Category: Shoichet, B K.]] | [[Category: Shoichet, B K.]] | ||
| - | [[Category: IM2]] | ||
[[Category: beta-lactamase]] | [[Category: beta-lactamase]] | ||
[[Category: carbapenem]] | [[Category: carbapenem]] | ||
[[Category: imipenem]] | [[Category: imipenem]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:04:09 2008'' |
Revision as of 19:04, 30 March 2008
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| , resolution 1.80Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | K12 (Escherichia coli) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Related: | 1KE4, 1FCO, 1BT5
| ||||||
| 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
