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Zinc in PDB 2bfz: Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in 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 20MM ZNSO4 in 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 20MM ZNSO4 in 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 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized., PDB code: 2bfz 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 (°) 67.309, 67.309, 177.604, 90.00, 90.00, 120.00
R / Rfree (%) 18.2 / 23.9

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 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized. (pdb code 2bfz). 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 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized., PDB code: 2bfz:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in 2bfz

Go back to Zinc Binding Sites List in 2bfz
Zinc binding site 1 out of 2 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in 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 20MM ZNSO4 in 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:21.4
occ:1.00
 ND1 A:HIS118 1.9 15.0 1.0
NE2 A:HIS116 2.1 14.8 1.0
NE2 A:HIS196 2.2 8.0 1.0
CG A:HIS118 2.9 17.3 1.0
CE1 A:HIS118 2.9 15.5 1.0
CE1 A:HIS116 3.0 14.3 1.0
CD2 A:HIS196 3.0 8.7 1.0
CD2 A:HIS116 3.1 13.2 1.0
OD1 A:CSD221 3.1 34.5 1.0
CB A:HIS118 3.3 17.8 1.0
CE1 A:HIS196 3.3 8.8 1.0
OD1 A:ASP120 3.8 27.2 1.0
NE2 A:HIS118 4.1 16.7 1.0
CD2 A:HIS118 4.1 16.6 1.0
ND1 A:HIS116 4.1 14.6 1.0
CG A:HIS116 4.2 14.3 1.0
CG A:HIS196 4.2 9.4 1.0
CB A:CSD221 4.3 24.7 1.0
ND1 A:HIS196 4.3 8.5 1.0
SG A:CSD221 4.3 34.9 1.0
CG2 A:THR197 4.4 11.7 1.0
OD2 A:ASP120 4.5 28.0 1.0
CG A:ASP120 4.6 27.6 1.0
CA A:HIS118 4.8 18.9 1.0
O A:HOH2130 5.0 32.3 1.0

Zinc binding site 2 out of 2 in 2bfz

Go back to Zinc Binding Sites List in 2bfz
Zinc binding site 2 out of 2 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in 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 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent. CYS221 Is Oxidized. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1297

b:17.8
occ:1.00
 NE2 B:HIS196 2.1 15.8 1.0
ND1 B:HIS118 2.2 17.8 1.0
NE2 B:HIS116 2.2 14.0 1.0
CD2 B:HIS196 3.0 15.2 1.0
CG B:HIS118 3.1 18.8 1.0
O B:HOH2082 3.1 20.5 1.0
CD2 B:HIS116 3.2 15.5 1.0
CE1 B:HIS196 3.2 17.0 1.0
CE1 B:HIS118 3.2 17.9 1.0
CE1 B:HIS116 3.3 15.2 1.0
CB B:HIS118 3.3 18.2 1.0
OD1 B:ASP120 4.0 33.6 1.0
SG B:CSO221 4.1 31.6 1.0
CG B:HIS196 4.2 14.8 1.0
CD2 B:HIS118 4.2 18.4 1.0
ND1 B:HIS196 4.2 15.4 1.0
NE2 B:HIS118 4.3 18.3 1.0
CB B:CSO221 4.3 23.1 1.0
CG B:HIS116 4.3 15.4 1.0
ND1 B:HIS116 4.3 16.0 1.0
OD2 B:ASP120 4.6 33.5 1.0
CG2 B:THR197 4.7 10.1 1.0
CG B:ASP120 4.7 31.5 1.0
CA B:HIS118 4.8 19.3 1.0
N1 B:AZI1294 4.8 42.2 1.0
N2 B:AZI1294 4.9 43.3 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 22:00:16 2024

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