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PDBe Entry: 2bg7 
BACILLUS CEREUS METALLO-BETA-LACTAMASE (BCII) ARG (121) CYS MUTANT. SOLVED AT PH4.5 USING 20 MICROMOLAR ZNSO4 IN THE BUFFER. 1MM DTT WAS USED AS A REDUCING AGENT. CYS221 IS OXIDIZED.
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HYDROLASE
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X-RAY DIFFRACTION
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Resolution: 2.1 Å, R-factor: 19.04%, Free R-factor: 22.2%, Spacegroup: P 31 2 1
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31/03/2005, deposition: 17/12/2004, last revision: 02/02/2010
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Davies, A.M.; Rasia, R.M.; Vila, A.J.; Sutton, B.J.; Fabiane, S.M.
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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 vol:44, pag:4841 (2005) [PubMed ID 15779910 ]
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HYDROLASE, ANTIBIOTIC RESISTANCE
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3.5.2.6 ExPASy BRENDA (A B)
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Bacillus cereus 1396(A B)
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Beta-lactamase 2 precursor (EC 3.5.2.6) (Beta-lactamase II) (Penicillinase) (Cephalosporinase) P04190 (A B)
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A, B
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1bc2, 1bmc, 1bvt, 1dxk, 1mqo, 2bc2, 2bfk, 2bfl, 2bfz, 2bg2, 2bg6, 2bg8, 2bga, 3bc2
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| A, B |
BETA-LACTAMASE II |
Protein |
P04190 (BLA2_BACCE)
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227 |
96% |
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| A, B |
GLYCEROL |
GOL
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| A, B |
ZINC ION |
ZN
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| A, B |
SULFATE ION |
SO4
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