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Zinc in PDB 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.

Enzymatic activity of 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.

All present enzymatic activity of 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.:
3.5.2.6;

Protein crystallography data

The structure of 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., PDB code: 2bga was solved by A.M.Davies, R.M.Rasia, A.J.Vila, B.J.Sutton, S.M.Fabiane, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 6.00 / 2.70
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.391, 67.391, 178.530, 90.00, 90.00, 120.00
R / Rfree (%) 18.6 / 24.8

Zinc Binding Sites:

The binding sites of Zinc atom in the 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. (pdb code 2bga). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the 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., PDB code: 2bga:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2bga

Go back to Zinc Binding Sites List in 2bga
Zinc binding site 1 out of 2 in the 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.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of 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. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1296

b:23.9
occ:1.00
 ND1 A:HIS118 2.0 18.3 1.0
NE2 A:HIS116 2.0 23.3 1.0
O A:HOH2110 2.1 4.8 1.0
NE2 A:HIS196 2.1 19.2 1.0
CG A:HIS118 2.9 17.9 1.0
CD2 A:HIS116 2.9 22.9 1.0
CE1 A:HIS118 2.9 18.7 1.0
CD2 A:HIS196 3.0 16.9 1.0
CE1 A:HIS116 3.0 24.1 1.0
CE1 A:HIS196 3.1 18.7 1.0
CB A:HIS118 3.3 18.9 1.0
OD1 A:CSD221 3.5 32.5 1.0
NE2 A:HIS118 4.0 18.9 1.0
OD1 A:ASP120 4.0 28.1 1.0
CD2 A:HIS118 4.0 17.9 1.0
CG A:HIS116 4.0 23.1 1.0
ND1 A:HIS116 4.1 24.0 1.0
CG A:HIS196 4.2 16.8 1.0
ND1 A:HIS196 4.2 17.7 1.0
CG2 A:THR197 4.3 13.9 1.0
CB A:CSD221 4.4 28.4 1.0
SG A:CSD221 4.6 34.9 1.0
OD2 A:ASP120 4.6 26.2 1.0
CA A:HIS118 4.7 17.7 1.0
CG A:ASP120 4.8 27.5 1.0
O A:HOH2082 4.9 10.6 1.0

Zinc binding site 2 out of 2 in 2bga

Go back to Zinc Binding Sites List in 2bga
Zinc binding site 2 out of 2 in the 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.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of 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. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1293

b:27.1
occ:1.00
 ND1 B:HIS118 2.0 22.9 1.0
O B:HOH2101 2.1 13.3 1.0
NE2 B:HIS196 2.1 21.9 1.0
NE2 B:HIS116 2.2 14.5 1.0
CD2 B:HIS196 2.8 21.8 1.0
CG B:HIS118 2.9 21.9 1.0
CE1 B:HIS118 3.1 23.5 1.0
CB B:HIS118 3.1 20.9 1.0
CD2 B:HIS116 3.1 14.9 1.0
CE1 B:HIS116 3.2 16.5 1.0
CE1 B:HIS196 3.3 22.5 1.0
OD1 B:CSD221 3.6 31.7 1.0
CD2 B:HIS118 4.0 23.5 1.0
CG B:HIS196 4.0 20.8 1.0
NE2 B:HIS118 4.1 24.6 1.0
OD1 B:ASP120 4.2 29.3 1.0
ND1 B:HIS196 4.2 21.2 1.0
CG B:HIS116 4.3 16.1 1.0
ND1 B:HIS116 4.3 16.0 1.0
CG2 B:THR197 4.4 9.9 1.0
CB B:CSD221 4.4 27.9 1.0
SG B:CSD221 4.6 33.9 1.0
CA B:HIS118 4.6 20.7 1.0
O B:HOH2043 4.6 31.7 1.0
OD2 B:ASP120 4.8 30.2 1.0
CG B:ASP120 4.9 26.9 1.0

Reference:

A.M.Davies, R.M.Rasia, A.J.Vila, B.J.Sutton, S.M.Fabiane. 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 V. 44 4841 2005.
ISSN: ISSN 0006-2960
PubMed: 15779910
DOI: 10.1021/BI047709T
Page generated: Wed Oct 16 22:01:34 2024

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