3bfg: Difference between revisions
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[[Image:3bfg.jpg|left|200px]] | [[Image:3bfg.jpg|left|200px]] | ||
'''class A beta-lactamase SED-G238C complexed with meropenem''' | {{Structure | ||
|PDB= 3bfg |SIZE=350|CAPTION= <scene name='initialview01'>3bfg</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MER:(1R,5S,6S)-2-[(3S,5S)-5-DIMETHYLAMINOCARBONYLPYRROLIDIN-3-YLTHIO]-6-[(R)-1-HYDROXYETHYL]-1-METHYLCARBAPEN-2-EM-3-CARBOXYLIC ACID'>MER</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= bla-SED-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67826 Citrobacter sedlakii]) | |||
}} | |||
'''class A beta-lactamase SED-G238C complexed with meropenem''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
3BFG is a [ | 3BFG is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_sedlakii Citrobacter sedlakii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFG OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14684905 14684905] | ||
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
[[Category: Citrobacter sedlakii]] | [[Category: Citrobacter sedlakii]] | ||
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[[Category: acyl-enzyme]] | [[Category: acyl-enzyme]] | ||
[[Category: beta-lactamase]] | [[Category: beta-lactamase]] | ||
[[Category: class | [[Category: class some]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: meropenem]] | [[Category: meropenem]] | ||
[[Category: sed-g238c]] | [[Category: sed-g238c]] | ||
''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 18:58:32 2008'' | ||
Revision as of 19:58, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bla-SED-1 (Citrobacter sedlakii) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
class A beta-lactamase SED-G238C complexed with meropenem
OverviewOverview
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 StructureAbout this Structure
3BFG is a Single protein structure of sequence from Citrobacter sedlakii. Full crystallographic information is available from OCA.
ReferenceReference
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
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