The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.
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.
D008958:Models, Molecular; D010405:Penicillinase; D011487:Protein Conformation; D013302:Streptomyces / Q000201:enzymology*; D014961:X-Ray Diffraction
D010405:Penicillinase