3bfc
From Proteopedia
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| - | [[Image:3bfc.jpg|left|200px]] | + | [[Image:3bfc.jpg|left|200px]] |
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| - | '''class A beta-lactamase SED-G238C complexed with imipenem''' | + | {{Structure |
| + | |PDB= 3bfc |SIZE=350|CAPTION= <scene name='initialview01'>3bfc</scene>, resolution 2.2Å | ||
| + | |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= 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 imipenem''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 3BFC is a [ | + | 3BFC 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=3BFC 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: imipenem]] | [[Category: imipenem]] | ||
[[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 18:58:28 2008'' |
Revision as of 16:58, 20 March 2008
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| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| 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 imipenem
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
3BFC 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
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