1bc2
ZN-DEPENDENT METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS
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OverviewOverview
The structure of the zinc-dependent beta-lactamase II from Bacillus cereus, has been determined at 1.9 A resolution in a crystal form with two, molecules in the asymmetric unit and 400 waters (space group P3121; Rcryst, = 20.8%). The active site contains two zinc ions: Zn1 is tightly, coordinated by His86, His88, and His149, while Zn2 is loosely coordinated, by Asp90, Cys168, and His210. A water molecule (W1) lies between the two, zinc ions but is significantly closer to Zn1 and at a distance of only 1.9, A is effectively a hydroxide moiety and a potential, preactivated, nucleophile. In fact, Asp90 bridges W1 to Zn2, and its location is thus, distinct from that of the bridging water molecules in the binuclear zinc, peptidases or other binuclear zinc hydrolases. Modeling of penicillin, ... [(full description)]
About this StructureAbout this Structure
1BC2 is a [Single protein] structure of sequence from [Bacillus cereus] with ZN and SO4 as [ligands]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Sites: ASA, ASB, ZNA and ZNB. Full crystallographic information is available from [OCA].
ReferenceReference
Crystal structure of the zinc-dependent beta-lactamase from Bacillus cereus at 1.9 A resolution: binuclear active site with features of a mononuclear enzyme., Fabiane SM, Sohi MK, Wan T, Payne DJ, Bateson JH, Mitchell T, Sutton BJ, Biochemistry. 1998 Sep 8;37(36):12404-11. PMID:9730812
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