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Zinc in PDB 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.

Enzymatic activity of 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.

All present enzymatic activity of 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.:
3.5.2.6;

Protein crystallography data

The structure of 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., PDB code: 2bg7 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 / 2.10
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.578, 67.578, 178.769, 90.00, 90.00, 120.00
R / Rfree (%) 19 / 22.2

Zinc Binding Sites:

The binding sites of Zinc atom in the 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. (pdb code 2bg7). 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 PH4.5 Using 20 Micromolar ZNSO4 in the Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized., PDB code: 2bg7:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2bg7

Go back to Zinc Binding Sites List in 2bg7
Zinc binding site 1 out of 2 in the 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.


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 PH4.5 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:Zn1299

b:52.7
occ:1.00
 O A:HOH2166 2.2 39.9 1.0
ND1 A:HIS118 2.4 34.7 1.0
NE2 A:HIS196 2.5 22.2 1.0
NE2 A:HIS116 2.6 28.6 1.0
CD2 A:HIS196 3.1 19.6 1.0
CD2 A:HIS116 3.1 25.7 1.0
CG A:HIS118 3.3 33.5 1.0
CE1 A:HIS118 3.4 34.1 1.0
CB A:HIS118 3.5 30.4 1.0
CE1 A:HIS196 3.7 21.6 1.0
CE1 A:HIS116 3.7 26.9 1.0
O A:HOH2064 3.9 53.7 1.0
OD1 A:ASP120 4.0 39.2 1.0
SG A:CSO221 4.2 37.1 1.0
CG2 A:THR197 4.2 11.8 1.0
CG A:HIS116 4.3 24.2 1.0
CG A:HIS196 4.4 19.0 1.0
CD2 A:HIS118 4.4 33.1 1.0
CB A:CSO221 4.4 24.4 1.0
NE2 A:HIS118 4.4 33.6 1.0
ND1 A:HIS116 4.6 26.7 1.0
ND1 A:HIS196 4.7 19.9 1.0
OD2 A:ASP120 4.7 40.0 1.0
CG A:ASP120 4.7 38.4 1.0
O1 A:GOL1294 4.8 46.6 1.0
O A:HOH2125 4.8 18.5 1.0
O2 A:GOL1294 4.8 44.9 1.0
O A:HOH2117 4.9 53.7 1.0
CA A:HIS118 4.9 28.6 1.0

Zinc binding site 2 out of 2 in 2bg7

Go back to Zinc Binding Sites List in 2bg7
Zinc binding site 2 out of 2 in the 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.


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 PH4.5 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:Zn1299

b:49.0
occ:1.00
 NE2 B:HIS196 2.4 25.9 1.0
NE2 B:HIS116 2.6 29.5 1.0
ND1 B:HIS118 2.7 34.6 1.0
O B:HOH2174 3.0 39.4 1.0
CD2 B:HIS196 3.1 24.2 1.0
CD2 B:HIS116 3.1 27.9 1.0
CE1 B:HIS196 3.5 26.3 1.0
CG B:HIS118 3.6 32.0 1.0
CB B:HIS118 3.6 28.5 1.0
CE1 B:HIS116 3.7 30.1 1.0
CE1 B:HIS118 3.7 35.0 1.0
SG B:CSO221 4.0 35.2 1.0
OD1 B:ASP120 4.0 33.0 1.0
CG B:HIS116 4.3 26.6 1.0
CB B:CSO221 4.3 26.3 1.0
CG B:HIS196 4.3 22.5 1.0
CG2 B:THR197 4.4 11.9 1.0
ND1 B:HIS196 4.5 23.9 1.0
OD2 B:ASP120 4.5 32.4 1.0
ND1 B:HIS116 4.5 28.0 1.0
CG B:ASP120 4.6 30.6 1.0
O1 B:GOL1296 4.7 44.0 1.0
CD2 B:HIS118 4.7 33.0 1.0
O2 B:GOL1296 4.7 42.5 1.0
O B:HOH2073 4.8 34.1 1.0
NE2 B:HIS118 4.8 34.2 1.0
OD B:CSO221 4.8 31.7 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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