2BGA
Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH7 using 20 Micromolar ZnSO4 in the buffer. 1mM DTT was used as a reducing agent. Cys221 is oxidized.
Summary for 2BGA
Entry DOI | 10.2210/pdb2bga/pdb |
Related | 1BC2 1BMC 1BVT 1DXK 1MQO 2BC2 2BFK 2BFL 2BFZ 2BG2 2BG6 2BG7 2BG8 3BC2 |
Descriptor | BETA-LACTAMASE II, AZIDE ION, GLYCEROL, ... (6 entities in total) |
Functional Keywords | hydrolase, zinc, metallo-beta-lactamase, antibiotic resistance |
Biological source | BACILLUS CEREUS |
Total number of polymer chains | 2 |
Total formula weight | 50910.36 |
Authors | Davies, A.M.,Rasia, R.M.,Vila, A.J.,Sutton, B.J.,Fabiane, S.M. (deposition date: 2004-12-17, release date: 2005-03-31, Last modification date: 2023-12-13) |
Primary citation | Davies, A.M.,Rasia, R.M.,Vila, A.J.,Sutton, B.J.,Fabiane, S.M. Effect of Ph on the Active Site of an Arg121Cys Mutant of the Metallo-Beta-Lactamase from Bacillus Cereus: Implications for the Enzyme Mechanism Biochemistry, 44:4841-, 2005 Cited by PubMed: 15779910DOI: 10.1021/BI047709T PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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