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Zinc in PDB 2bfk: Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent

Enzymatic activity of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent

All present enzymatic activity of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent:
3.5.2.6;

Protein crystallography data

The structure of Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent, PDB code: 2bfk 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 / 2.00
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.311, 67.311, 178.010, 90.00, 90.00, 120.00
R / Rfree (%) 17.2 / 20.9

Zinc Binding Sites:

The binding sites of Zinc atom in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent (pdb code 2bfk). 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 PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent, PDB code: 2bfk:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2bfk

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Zinc binding site 1 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent


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 PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1300

b:22.0
occ:1.00
 ND1 A:HIS118 1.9 18.2 1.0
O A:HOH2258 1.9 24.7 1.0
NE2 A:HIS196 2.1 16.3 1.0
NE2 A:HIS116 2.1 18.9 1.0
CE1 A:HIS118 2.8 18.0 1.0
CG A:HIS118 2.9 20.1 1.0
CD2 A:HIS196 2.9 14.1 1.0
O A:HOH2259 2.9 47.9 1.0
CE1 A:HIS116 3.1 19.6 1.0
CD2 A:HIS116 3.1 18.0 1.0
CE1 A:HIS196 3.1 15.9 1.0
CB A:HIS118 3.3 21.0 1.0
ZN A:ZN1301 3.6 51.6 1.0
NE2 A:HIS118 3.9 19.8 1.0
OD1 A:ASP120 3.9 26.3 1.0
CD2 A:HIS118 4.0 19.8 1.0
CG A:HIS196 4.1 15.6 1.0
O1 A:GOL1295 4.2 56.2 1.0
ND1 A:HIS116 4.2 19.0 1.0
SG A:CYS221 4.2 33.7 1.0
ND1 A:HIS196 4.2 14.4 1.0
CB A:CYS221 4.2 22.7 1.0
CG A:HIS116 4.2 18.4 1.0
CG2 A:THR197 4.3 12.1 1.0
C3 A:GOL1295 4.6 56.6 1.0
CG A:ASP120 4.8 26.8 1.0
CA A:HIS118 4.8 21.6 1.0
OD2 A:ASP120 4.9 28.2 1.0
C1 A:GOL1295 4.9 57.0 1.0
O A:HOH2101 5.0 39.9 1.0

Zinc binding site 2 out of 4 in 2bfk

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Zinc binding site 2 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent


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 PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn1301

b:51.6
occ:1.00
 O1 A:GOL1295 2.0 56.2 1.0
O A:HOH2258 2.1 24.7 1.0
SG A:CYS221 2.4 33.7 1.0
NE2 A:HIS263 2.5 26.6 1.0
OD2 A:ASP120 2.6 28.2 1.0
CD2 A:HIS263 3.1 25.5 1.0
C1 A:GOL1295 3.3 57.0 1.0
CG A:ASP120 3.3 26.8 1.0
OD1 A:ASP120 3.5 26.3 1.0
CB A:CYS221 3.5 22.7 1.0
ZN A:ZN1300 3.6 22.0 1.0
CE1 A:HIS263 3.6 27.1 1.0
C3 A:GOL1295 3.8 56.6 1.0
O A:HOH2103 4.0 43.3 1.0
C2 A:GOL1295 4.0 57.0 1.0
O A:HOH2259 4.0 47.9 1.0
O A:HOH2101 4.4 39.9 1.0
O2 A:GOL1295 4.4 57.8 1.0
NE2 A:HIS196 4.4 16.3 1.0
CG A:HIS263 4.4 24.4 1.0
CE1 A:HIS116 4.5 19.6 1.0
CB A:ASP120 4.6 25.0 1.0
ND1 A:HIS263 4.6 26.8 1.0
NE2 A:HIS116 4.6 18.9 1.0
CA A:CYS221 4.7 18.4 1.0
O A:HOH2184 4.8 41.8 1.0
CE1 A:HIS196 4.8 15.9 1.0

Zinc binding site 3 out of 4 in 2bfk

Go back to Zinc Binding Sites List in 2bfk
Zinc binding site 3 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent


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 PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1299

b:21.6
occ:1.00
 O B:HOH2243 2.0 21.4 1.0
ND1 B:HIS118 2.0 21.5 1.0
NE2 B:HIS196 2.1 15.1 1.0
NE2 B:HIS116 2.2 18.4 1.0
CD2 B:HIS196 2.9 13.8 1.0
CG B:HIS118 3.0 22.2 1.0
CE1 B:HIS118 3.0 22.8 1.0
CD2 B:HIS116 3.1 17.8 1.0
O B:HOH2113 3.1 47.8 1.0
CE1 B:HIS116 3.2 18.8 1.0
CE1 B:HIS196 3.2 14.0 1.0
CB B:HIS118 3.3 20.3 1.0
ZN B:ZN1300 3.6 48.6 1.0
OD1 B:ASP120 4.0 30.8 1.0
SG B:CYS221 4.0 33.3 1.0
NE2 B:HIS118 4.1 22.9 1.0
CD2 B:HIS118 4.1 22.1 1.0
CB B:CYS221 4.1 23.6 1.0
CG B:HIS196 4.1 12.8 1.0
ND1 B:HIS196 4.2 13.8 1.0
CG B:HIS116 4.2 16.7 1.0
ND1 B:HIS116 4.3 18.0 1.0
CG2 B:THR197 4.5 11.5 1.0
N1 B:AZI1292 4.6 40.1 1.0
OD2 B:ASP120 4.7 31.2 1.0
CG B:ASP120 4.8 28.1 1.0
CA B:HIS118 4.8 19.4 1.0
N2 B:AZI1292 5.0 42.2 1.0

Zinc binding site 4 out of 4 in 2bfk

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Zinc binding site 4 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent


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 PH7 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Zn1300

b:48.6
occ:1.00
 SG B:CYS221 2.1 33.3 1.0
O B:HOH2243 2.3 21.4 1.0
NE2 B:HIS263 2.5 31.0 1.0
O B:HOH2177 2.8 35.7 1.0
OD2 B:ASP120 2.8 31.2 1.0
CB B:CYS221 3.2 23.6 1.0
N1 B:AZI1292 3.2 40.1 1.0
CD2 B:HIS263 3.4 29.9 1.0
CE1 B:HIS263 3.5 29.5 1.0
ZN B:ZN1299 3.6 21.6 1.0
CG B:ASP120 3.7 28.1 1.0
OD1 B:ASP120 3.9 30.8 1.0
N2 B:AZI1292 4.0 42.2 1.0
NE2 B:HIS196 4.1 15.1 1.0
O B:HOH2113 4.2 47.8 1.0
O B:HOH2057 4.3 40.0 1.0
CA B:CYS221 4.4 19.4 1.0
CE1 B:HIS196 4.5 14.0 1.0
CG B:HIS263 4.6 28.8 1.0
ND1 B:HIS263 4.6 30.8 1.0
NE2 B:HIS116 4.6 18.4 1.0
CE1 B:HIS116 4.6 18.8 1.0
N3 B:AZI1292 4.8 40.7 1.0
CD2 B:HIS196 4.8 13.8 1.0
CB B:ASP120 4.9 25.1 1.0
O B:HOH2242 5.0 53.4 1.0
N B:CYS221 5.0 16.5 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 03:18:22 2020

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