3bff
From Proteopedia
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'''class A beta-lactamase SED-G238C complexed with faropenem''' | '''class A beta-lactamase SED-G238C complexed with faropenem''' | ||
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[[Category: Petrella, S.]] | [[Category: Petrella, S.]] | ||
[[Category: Sougakoff, W.]] | [[Category: Sougakoff, W.]] | ||
| - | [[Category: | + | [[Category: Acyl-enzyme]] |
| - | [[Category: | + | [[Category: Beta-lactamase]] |
| - | [[Category: | + | [[Category: Class a sed-g238c]] |
| - | [[Category: | + | [[Category: Faropenem]] |
| - | [[Category: | + | [[Category: Hydrolase]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:43:00 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 17:43, 4 May 2008
class A beta-lactamase SED-G238C complexed with faropenem
Overview
SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type extended-spectrum beta-lactamase that has the ability to hydrolyze expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED mutant in which Gly238 has been replaced by a cysteine, forming a disulfide bridge with the other Cys residue located at position 69 (SED-G238C), have been crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 188.09, b = 73.65, c = 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c = 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray diffraction data were collected to maximum resolutions of 2.4 A for SED-1 and 2.0 A for SED-G238C.
About this Structure
3BFF is a Single protein structure of sequence from Citrobacter sedlakii. Full crystallographic information is available from OCA.
Reference
Crystallization and preliminary X-ray diffraction study of the class A beta-lactamase SED-1 and its mutant SED-G238C from Citrobacter sedlakii., Petrella S, Pernot L, Sougakoff W, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):125-8. Epub 2003, Dec 18. PMID:14684905 Page seeded by OCA on Sun May 4 20:43:00 2008
