3bfg: Difference between revisions

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<StructureSection load='3bfg' size='340' side='right'caption='[[3bfg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3bfg' size='340' side='right'caption='[[3bfg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3bfg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_51115 Atcc 51115]. 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>
<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>
</td></tr><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>
</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>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bfc|3bfc]], [[3bfd|3bfd]], [[3bfe|3bfe]], [[3bff|3bff]]</div></td></tr>
<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>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">bla-SED-1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=67826 ATCC 51115])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span></td></tr>
<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>
<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>
</table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93PQ0_9ENTR Q93PQ0_9ENTR]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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].
</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].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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<ref>PMID:14684905</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3bfg" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Atcc 51115]]
[[Category: Citrobacter sedlakii]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Pernot, L]]
[[Category: Pernot L]]
[[Category: Petrella, S]]
[[Category: Petrella S]]
[[Category: Sougakoff, W]]
[[Category: Sougakoff W]]
[[Category: Acyl-enzyme]]
[[Category: Class some]]
[[Category: Hydrolase]]
[[Category: Meropenem]]
[[Category: Sed-g238c]]

Revision as of 17:45, 1 November 2023

class A beta-lactamase SED-G238C complexed with meropenemclass A beta-lactamase SED-G238C complexed with meropenem

Structural highlights

3bfg is a 4 chain structure with sequence from Citrobacter sedlakii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q93PQ0_9ENTR

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3bfg, resolution 2.00Å

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