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1bsg
From Proteopedia
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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
Page seeded by OCA on Tue Nov 20 11:53:05 2007
