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Zinc in PDB 2bg2: Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.

Enzymatic activity of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.

All present enzymatic activity of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.:
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 the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced., PDB code: 2bg2 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 / 2.40
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.300, 67.300, 177.183, 90.00, 90.00, 120.00
R / Rfree (%) 17.9 / 22.4

Other elements in 2bg2:

The structure of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced. also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

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 the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced. (pdb code 2bg2). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 4 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 the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced., PDB code: 2bg2:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2bg2

Go back to Zinc Binding Sites List in 2bg2
Zinc binding site 1 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.


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 the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1301

b:26.4
occ:1.00
 ND1 A:HIS118 2.0 21.9 1.0
NE2 A:HIS196 2.0 15.7 1.0
NE2 A:HIS116 2.2 20.1 1.0
CD2 A:HIS196 2.9 15.7 1.0
O2 A:GOL1296 2.9 44.0 1.0
CE1 A:HIS118 3.0 24.1 1.0
CG A:HIS118 3.0 23.5 1.0
CE1 A:HIS196 3.1 16.6 1.0
CE1 A:HIS116 3.1 21.2 1.0
C1 A:GOL1296 3.2 45.5 1.0
CD2 A:HIS116 3.2 20.5 1.0
CB A:HIS118 3.3 23.3 1.0
O1 A:GOL1296 3.4 44.7 1.0
C2 A:GOL1296 3.5 45.1 1.0
C3 A:GOL1296 3.6 45.6 1.0
SG A:CYS221 3.7 33.5 1.0
ZN A:ZN1302 4.0 47.3 1.0
OD1 A:ASP120 4.0 29.6 1.0
NE2 A:HIS118 4.1 23.5 1.0
CG A:HIS196 4.1 16.3 1.0
CB A:CYS221 4.1 24.2 1.0
CD2 A:HIS118 4.1 23.3 1.0
ND1 A:HIS196 4.2 15.7 1.0
ND1 A:HIS116 4.3 20.8 1.0
CG A:HIS116 4.3 19.9 1.0
CG2 A:THR197 4.4 14.1 1.0
OD2 A:ASP120 4.6 28.9 1.0
CG A:ASP120 4.7 27.7 1.0
CA A:HIS118 4.8 23.4 1.0

Zinc binding site 2 out of 4 in 2bg2

Go back to Zinc Binding Sites List in 2bg2
Zinc binding site 2 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.


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 the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1302

b:47.3
occ:1.00
 NE2 A:HIS263 2.4 27.8 1.0
SG A:CYS221 2.4 33.5 1.0
O A:HOH2156 2.5 15.2 1.0
O2 A:GOL1296 2.7 44.0 1.0
CD2 A:HIS263 3.0 26.6 1.0
CB A:CYS221 3.2 24.2 1.0
O1 A:GOL1296 3.6 44.7 1.0
CE1 A:HIS263 3.6 26.8 1.0
OD2 A:ASP120 3.8 28.9 1.0
C2 A:GOL1296 3.8 45.1 1.0
ZN A:ZN1301 4.0 26.4 1.0
CE1 A:HIS196 4.1 16.6 1.0
NE2 A:HIS196 4.1 15.7 1.0
CA A:CYS221 4.2 21.9 1.0
C1 A:GOL1296 4.2 45.5 1.0
CG A:HIS263 4.3 25.3 1.0
O A:HOH2152 4.4 42.2 1.0
NZ A:LYS224 4.4 25.0 1.0
ND1 A:HIS263 4.5 27.2 1.0
O A:HOH2056 4.6 35.2 1.0
CG A:ASP120 4.7 27.7 1.0
C3 A:GOL1296 4.7 45.6 1.0
O A:HOH2113 4.8 17.8 1.0
ND1 A:HIS196 4.8 15.7 1.0
CD2 A:HIS196 4.9 15.7 1.0

Zinc binding site 3 out of 4 in 2bg2

Go back to Zinc Binding Sites List in 2bg2
Zinc binding site 3 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 3 of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1301

b:43.4
occ:1.00
 NE2 B:HIS263 2.3 27.3 1.0
O B:HOH2141 2.4 7.5 1.0
SG B:CYS221 2.5 31.9 1.0
CL B:CL1303 3.1 42.0 1.0
CD2 B:HIS263 3.2 26.2 1.0
CB B:CYS221 3.2 23.9 1.0
CE1 B:HIS263 3.4 25.2 1.0
O B:HOH2103 3.6 27.2 1.0
OD2 B:ASP120 3.8 29.5 1.0
ZN B:ZN1302 4.1 23.7 1.0
CE1 B:HIS196 4.1 16.8 1.0
NE2 B:HIS196 4.2 17.0 1.0
CA B:CYS221 4.3 20.4 1.0
CG B:HIS263 4.4 25.8 1.0
ND1 B:HIS263 4.4 26.4 1.0
NZ B:LYS224 4.5 19.4 1.0
CG B:ASP120 4.6 27.6 1.0
O B:HOH2096 4.7 20.0 1.0
O B:HOH2097 4.8 36.2 1.0
OD1 B:ASP120 4.8 31.0 1.0
ND1 B:HIS196 4.9 16.6 1.0

Zinc binding site 4 out of 4 in 2bg2

Go back to Zinc Binding Sites List in 2bg2
Zinc binding site 4 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced.


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 4 of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH4.5 Using 20MM ZNSO4 in the Buffer. 1MM Dtt and 1MM Tcep- Hcl Were Used As Reducing Agents. CYS221 Is Reduced. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1302

b:23.7
occ:1.00
 NE2 B:HIS196 2.1 17.0 1.0
ND1 B:HIS118 2.2 22.2 1.0
NE2 B:HIS116 2.3 18.7 1.0
CL B:CL1303 2.8 42.0 1.0
CD2 B:HIS196 3.1 16.5 1.0
CG B:HIS118 3.1 22.5 1.0
CD2 B:HIS116 3.2 20.8 1.0
CE1 B:HIS196 3.2 16.8 1.0
CE1 B:HIS118 3.2 22.1 1.0
CE1 B:HIS116 3.3 19.7 1.0
CB B:HIS118 3.3 21.5 1.0
OD1 B:ASP120 3.8 31.0 1.0
SG B:CYS221 3.9 31.9 1.0
ZN B:ZN1301 4.1 43.4 1.0
CG B:HIS196 4.2 16.8 1.0
CB B:CYS221 4.2 23.9 1.0
ND1 B:HIS196 4.3 16.6 1.0
CD2 B:HIS118 4.3 23.0 1.0
NE2 B:HIS118 4.3 22.2 1.0
CG B:HIS116 4.4 20.7 1.0
ND1 B:HIS116 4.4 20.9 1.0
CG2 B:THR197 4.6 14.1 1.0
CG B:ASP120 4.6 27.6 1.0
OD2 B:ASP120 4.7 29.5 1.0
O B:HOH2138 4.8 27.4 1.0
CA B:HIS118 4.8 22.0 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 22:00:36 2024

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