1bsg
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| , resolution 1.85Å | |||||||
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| Ligands: | |||||||
| Activity: | Beta-lactamase, with EC number 3.5.2.6 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BETA-LACTAMASE FROM STREPTOMYCES ALBUS G
OverviewOverview
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 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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