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Zinc in PDB 2bg8: Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20 Micromolar ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep-Hcl Were Used As Reducing Agents.

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 and 1MM Tcep-Hcl Were Used As Reducing Agents.

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 and 1MM Tcep-Hcl Were Used As Reducing Agents.:
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 and 1MM Tcep-Hcl Were Used As Reducing Agents., PDB code: 2bg8 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 / 2.50
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.250, 67.250, 177.800, 90.00, 90.00, 120.00
R / Rfree (%) 18.5 / 23.7

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 and 1MM Tcep-Hcl Were Used As Reducing Agents. (pdb code 2bg8). 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 and 1MM Tcep-Hcl Were Used As Reducing Agents., PDB code: 2bg8:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2bg8

Go back to Zinc Binding Sites List in 2bg8
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 and 1MM Tcep-Hcl Were Used As Reducing Agents.


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 and 1MM Tcep-Hcl Were Used As Reducing Agents. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1298

b:28.0
occ:1.00
 ND1 A:HIS118 2.0 25.8 1.0
NE2 A:HIS196 2.1 19.2 1.0
O A:HOH2136 2.3 22.3 1.0
NE2 A:HIS116 2.4 20.9 1.0
CD2 A:HIS196 2.9 17.9 1.0
CE1 A:HIS118 3.0 25.1 1.0
CG A:HIS118 3.0 26.6 1.0
CE1 A:HIS196 3.1 18.6 1.0
CD2 A:HIS116 3.2 20.9 1.0
CE1 A:HIS116 3.3 22.3 1.0
CB A:HIS118 3.4 26.2 1.0
OD1 A:ASP120 3.9 31.4 1.0
SG A:CSO221 4.0 37.8 1.0
O1 A:SO41302 4.0 81.0 1.0
NE2 A:HIS118 4.1 27.0 1.0
CG A:HIS196 4.1 17.8 1.0
CD2 A:HIS118 4.1 26.8 1.0
ND1 A:HIS196 4.2 18.0 1.0
O2 A:SO41302 4.2 81.9 1.0
CB A:CSO221 4.2 28.8 1.0
CG2 A:THR197 4.3 12.9 1.0
CG A:HIS116 4.4 19.5 1.0
O A:HOH2040 4.4 49.4 1.0
ND1 A:HIS116 4.4 21.2 1.0
S A:SO41302 4.7 81.4 1.0
CG A:ASP120 4.8 31.6 1.0
OD A:CSO221 4.8 36.5 1.0
OD2 A:ASP120 4.8 31.6 1.0
O A:HOH2098 4.8 20.5 1.0
CA A:HIS118 4.9 25.7 1.0

Zinc binding site 2 out of 2 in 2bg8

Go back to Zinc Binding Sites List in 2bg8
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 and 1MM Tcep-Hcl Were Used As Reducing Agents.


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 and 1MM Tcep-Hcl Were Used As Reducing Agents. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1297

b:37.4
occ:1.00
 NE2 B:HIS196 2.1 18.1 1.0
NE2 B:HIS116 2.3 20.1 1.0
ND1 B:HIS118 2.5 21.3 1.0
CD2 B:HIS196 3.1 16.4 1.0
CE1 B:HIS196 3.1 16.9 1.0
CD2 B:HIS116 3.2 20.7 1.0
CE1 B:HIS116 3.3 20.7 1.0
CG B:HIS118 3.3 20.7 1.0
CE1 B:HIS118 3.5 22.2 1.0
CB B:HIS118 3.5 20.5 1.0
SG B:CYS221 3.8 32.1 1.0
O2 B:SO41302 3.9 99.9 1.0
OD1 B:ASP120 3.9 31.7 1.0
CB B:CYS221 4.2 24.0 1.0
ND1 B:HIS196 4.2 15.4 1.0
CG B:HIS196 4.2 15.7 1.0
O4 B:SO41302 4.3 0.0 1.0
CG B:HIS116 4.4 21.2 1.0
ND1 B:HIS116 4.4 22.1 1.0
OD2 B:ASP120 4.5 31.2 1.0
CD2 B:HIS118 4.5 21.1 1.0
NE2 B:HIS118 4.6 23.0 1.0
O B:HOH2062 4.6 41.6 1.0
CG B:ASP120 4.6 29.0 1.0
S B:SO41302 4.6 99.4 1.0
CG2 B:THR197 4.7 12.2 1.0
CA B:HIS118 5.0 19.7 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 22:01:13 2024

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