1BSG

BETA-LACTAMASE FROM STREPTOMYCES ALBUS G

Summary for 1BSG

• Entry DOI: 10.2210/pdb1bsg/pdb
• Descriptor: BETA LACTAMASE, ACETATE ION (3 entities in total)
• Functional Keywords: hydrolase, antibiotic resistance, penicillin
• Biological source: Streptomyces albus
• Total number of polymer chains: 1
• Total formula weight: 28811.06

Authors

Fonze, E.,Charlier, P.,Dideberg, O. (deposition date: 1998-07-20, release date: 1999-01-13, Last modification date: 2024-02-07)

Primary citation

The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.
Biochem.J., 245:911-913, 1987

PubMed Abstract: 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.

PubMed: 3499147

Experimental method

X-RAY DIFFRACTION (1.85 Å)