1bsg: Difference between revisions

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{{STRUCTURE_1bsg|  PDB=1bsg  |  SCENE=  }}  
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'''BETA-LACTAMASE FROM STREPTOMYCES ALBUS G'''
===BETA-LACTAMASE FROM STREPTOMYCES ALBUS G===




==Overview==
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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.
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{{ABSTRACT_PUBMED_3499147}}


==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Penicillin]]
[[Category: Penicillin]]
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Revision as of 19:39, 30 June 2008

File:1bsg.png

Template:STRUCTURE 1bsg

BETA-LACTAMASE FROM STREPTOMYCES ALBUS GBETA-LACTAMASE FROM STREPTOMYCES ALBUS G

Template:ABSTRACT PUBMED 3499147

About this StructureAbout this Structure

1BSG is a Single protein structure of sequence from Streptomyces albus g. Full crystallographic information is available from OCA.

ReferenceReference

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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