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Zinc in PDB 2bg6: Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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 PH5 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 PH5 Using 20 Micromolar ZNSO4 in the Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized., PDB code: 2bg6 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 / 2.30
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.866, 67.866, 178.470, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 22.3

Zinc Binding Sites:

The binding sites of Zinc atom in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 Using 20 Micromolar ZNSO4 in the Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized. (pdb code 2bg6). 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 PH5 Using 20 Micromolar ZNSO4 in the Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized., PDB code: 2bg6:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2bg6

Go back to Zinc Binding Sites List in 2bg6
Zinc binding site 1 out of 2 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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:Zn1301

b:29.2
occ:1.00
 ND1 A:HIS118 2.1 27.8 1.0
O A:HOH2134 2.2 28.4 1.0
NE2 A:HIS116 2.2 20.5 1.0
NE2 A:HIS196 2.3 16.7 1.0
CD2 A:HIS116 3.0 20.4 1.0
CG A:HIS118 3.0 27.6 1.0
CD2 A:HIS196 3.1 16.1 1.0
CE1 A:HIS118 3.1 28.9 1.0
CB A:HIS118 3.3 26.6 1.0
CE1 A:HIS116 3.3 21.4 1.0
CE1 A:HIS196 3.4 17.3 1.0
OD1 A:CSD221 3.7 35.4 1.0
OD1 A:ASP120 3.9 36.4 1.0
CG A:HIS116 4.2 19.1 1.0
CD2 A:HIS118 4.2 26.5 1.0
NE2 A:HIS118 4.2 28.5 1.0
ND1 A:HIS116 4.3 20.4 1.0
CG A:HIS196 4.3 15.1 1.0
CG2 A:THR197 4.3 11.9 1.0
ND1 A:HIS196 4.4 17.0 1.0
CB A:CSD221 4.5 26.9 1.0
OD2 A:ASP120 4.7 37.8 1.0
CG A:ASP120 4.7 36.0 1.0
SG A:CSD221 4.7 36.9 1.0
CA A:HIS118 4.7 25.9 1.0
O A:HOH2100 4.9 15.2 1.0

Zinc binding site 2 out of 2 in 2bg6

Go back to Zinc Binding Sites List in 2bg6
Zinc binding site 2 out of 2 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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:Zn1301

b:28.3
occ:1.00
 NE2 B:HIS196 2.1 15.4 1.0
O B:HOH2162 2.1 34.6 1.0
ND1 B:HIS118 2.2 21.6 1.0
NE2 B:HIS116 2.3 18.5 1.0
CD2 B:HIS196 2.9 14.7 1.0
CG B:HIS118 3.1 21.8 1.0
O B:HOH2159 3.2 32.2 1.0
CE1 B:HIS118 3.2 20.6 1.0
CD2 B:HIS116 3.2 18.3 1.0
CE1 B:HIS196 3.2 15.4 1.0
OD1 B:CSD221 3.3 36.2 1.0
CE1 B:HIS116 3.4 20.0 1.0
CB B:HIS118 3.4 21.2 1.0
OD1 B:ASP120 4.0 34.4 1.0
CG B:HIS196 4.1 14.9 1.0
ND1 B:HIS196 4.2 16.0 1.0
CD2 B:HIS118 4.3 20.9 1.0
NE2 B:HIS118 4.3 21.5 1.0
CG B:HIS116 4.4 18.8 1.0
CB B:CSD221 4.4 27.1 1.0
ND1 B:HIS116 4.4 19.4 1.0
SG B:CSD221 4.5 36.8 1.0
CG2 B:THR197 4.5 10.6 1.0
O B:HOH2070 4.7 46.0 1.0
CA B:HIS118 4.9 21.0 1.0
CG B:ASP120 4.9 32.2 1.0
O B:HOH2103 5.0 20.0 1.0
OD2 B:ASP120 5.0 35.4 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 22:00:56 2024

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