Atomistry » Zinc » PDB 2b65-2bmi » 2bg7
Atomistry »
  Zinc »
    PDB 2b65-2bmi »
      2bg7 »

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 Dec 16 03:18:24 2020

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy