3bfg

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[[Image:3bfg.jpg|left|200px]]
 
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{{Structure
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==class A beta-lactamase SED-G238C complexed with meropenem==
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|PDB= 3bfg |SIZE=350|CAPTION= <scene name='initialview01'>3bfg</scene>, resolution 2.0&Aring;
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<StructureSection load='3bfg' size='340' side='right'caption='[[3bfg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|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>
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<table><tr><td colspan='2'>[[3bfg]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BFG FirstGlance]. <br>
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|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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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|GENE= bla-SED-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67826 Citrobacter sedlakii])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MER:(4R,5S)-3-{[(3S,5S)-5-(DIMETHYLCARBAMOYL)PYRROLIDIN-3-YL]SULFANYL}-5-[(2S,3R)-3-HYDROXY-1-OXOBUTAN-2-YL]-4-METHYL-4,5-DIHYDRO-1H-PYRROLE-2-CARBOXYLIC+ACID'>MER</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfg OCA], [https://pdbe.org/3bfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bfg RCSB], [https://www.ebi.ac.uk/pdbsum/3bfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bfg ProSAT]</span></td></tr>
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|RELATEDENTRY=[[3bfc|3BFC]], [[3bfd|3BFD]], [[3bfe|3BFE]], [[3bff|3BFF]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfg OCA], [http://www.ebi.ac.uk/pdbsum/3bfg PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bfg RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/Q93PQ0_9ENTR Q93PQ0_9ENTR]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bf/3bfg_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3bfg ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''class A beta-lactamase SED-G238C complexed with meropenem'''
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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:014684905<ref>PMID:014684905</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3bfg" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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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].
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__TOC__
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</StructureSection>
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==Reference==
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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]
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[[Category: Beta-lactamase]]
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[[Category: Citrobacter sedlakii]]
[[Category: Citrobacter sedlakii]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Pernot, L.]]
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[[Category: Pernot L]]
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[[Category: Petrella, S.]]
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[[Category: Petrella S]]
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[[Category: Sougakoff, W.]]
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[[Category: Sougakoff W]]
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[[Category: acyl-enzyme]]
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[[Category: beta-lactamase]]
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[[Category: class some]]
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[[Category: hydrolase]]
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[[Category: meropenem]]
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[[Category: sed-g238c]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:25:50 2008''
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Current revision

class A beta-lactamase SED-G238C complexed with meropenem

PDB ID 3bfg

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