1bsg: Difference between revisions
New page: left|200px<br /><applet load="1bsg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bsg, resolution 1.85Å" /> '''BETA-LACTAMASE FROM ... |
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[[Image:1bsg.gif|left|200px]]<br /><applet load="1bsg" size=" | [[Image:1bsg.gif|left|200px]]<br /><applet load="1bsg" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1bsg, resolution 1.85Å" /> | caption="1bsg, resolution 1.85Å" /> | ||
'''BETA-LACTAMASE FROM STREPTOMYCES ALBUS G'''<br /> | '''BETA-LACTAMASE FROM STREPTOMYCES ALBUS G'''<br /> | ||
==Overview== | ==Overview== | ||
The crystal structure of the beta-lactamase of Streptomyces albus G has | 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. | ||
==About this Structure== | ==About this Structure== | ||
1BSG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus_g Streptomyces albus g] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | 1BSG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_albus_g Streptomyces albus g] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BSG OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: penicillin]] | [[Category: penicillin]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:58:36 2008'' | ||
Revision as of 09:58, 21 February 2008
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BETA-LACTAMASE FROM STREPTOMYCES ALBUS G
Overview
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.
About this Structure
1BSG is a Single protein structure of sequence from Streptomyces albus g with ACT as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
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
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