Atomistry » Zinc » PDB 2b8k-2bnm » 2bg6
Atomistry »
  Zinc »
    PDB 2b8k-2bnm »
      2bg6 »

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

Last articles

Zn in 9MJ5
Zn in 9HNW
Zn in 9G0L
Zn in 9FNE
Zn in 9DZN
Zn in 9E0I
Zn in 9D32
Zn in 9DAK
Zn in 8ZXC
Zn in 8ZUF
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy