1bsg

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[[Image:1bsg.gif|left|200px]]
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{{STRUCTURE_1bsg| PDB=1bsg | SCENE= }}
{{STRUCTURE_1bsg| PDB=1bsg | SCENE= }}
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'''BETA-LACTAMASE FROM STREPTOMYCES ALBUS G'''
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===BETA-LACTAMASE FROM STREPTOMYCES ALBUS G===
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==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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(as it appears on PubMed at http://www.pubmed.gov), where 3499147 is the PubMed ID number.
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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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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:54:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:39:14 2008''

Revision as of 16:39, 30 June 2008

Image:1bsg.png

Template:STRUCTURE 1bsg

BETA-LACTAMASE FROM STREPTOMYCES ALBUS G

Template:ABSTRACT PUBMED 3499147

About this Structure

1BSG is a Single protein structure of sequence from Streptomyces albus g. 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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