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3bfc
From Proteopedia
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|PDB= 3bfc |SIZE=350|CAPTION= <scene name='initialview01'>3bfc</scene>, resolution 2.2Å | |PDB= 3bfc |SIZE=350|CAPTION= <scene name='initialview01'>3bfc</scene>, resolution 2.2Å | ||
|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= bla-SED-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67826 Citrobacter sedlakii]) | |GENE= bla-SED-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67826 Citrobacter sedlakii]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[3bfd|3BFD]], [[3bfe|3BFE]], [[3bff|3BFF]], [[3bfg|3BFG]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfc OCA], [http://www.ebi.ac.uk/pdbsum/3bfc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bfc RCSB]</span> | ||
}} | }} | ||
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[[Category: Petrella, S.]] | [[Category: Petrella, S.]] | ||
[[Category: Sougakoff, W.]] | [[Category: Sougakoff, W.]] | ||
| - | [[Category: IM2]] | ||
[[Category: acyl-enzyme]] | [[Category: acyl-enzyme]] | ||
[[Category: beta-lactamase]] | [[Category: beta-lactamase]] | ||
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[[Category: sed-g238c]] | [[Category: sed-g238c]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:25:47 2008'' |
Revision as of 02:25, 31 March 2008
| |||||||
| , resolution 2.2Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | bla-SED-1 (Citrobacter sedlakii) | ||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Related: | 3BFD, 3BFE, 3BFF, 3BFG
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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