Atomistry » Zinc » PDB 2b65-2bmi » 2bg2
Atomistry »
  Zinc »
    PDB 2b65-2bmi »
      2bg2 »

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 Dec 16 03:18:23 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