View source for 1bsg

==BETA-LACTAMASE FROM STREPTOMYCES ALBUS G==
<StructureSection load='1bsg' size='340' side='right' caption='[[1bsg]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bsg]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus Streptomyces albus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BSG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BSG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bsg RCSB], [http://www.ebi.ac.uk/pdbsum/1bsg PDBsum]</span></td></tr>
</table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/1bsg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains.

The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.,Dideberg O, Charlier P, Wery JP, Dehottay P, Dusart J, Erpicum T, Frere JM, Ghuysen JM Biochem J. 1987 Aug 1;245(3):911-3. PMID:3499147<ref>PMID:3499147</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>

==See Also==
*[[Beta-lactamase|Beta-lactamase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Beta-lactamase]]
[[Category: Streptomyces albus]]
[[Category: Charlier, P]]
[[Category: Dideberg, O]]
[[Category: Fonze, E]]
[[Category: Antibiotic resistance]]
[[Category: Hydrolase]]
[[Category: Penicillin]]