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Zinc in PDB 2bfl: Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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 PH5 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 PH5 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent., PDB code: 2bfl 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 / 1.80
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 67.535, 67.535, 178.712, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 20.2

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 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent. (pdb code 2bfl). 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 PH5 Using 20MM ZNSO4 in Buffer. 1MM Dtt Was Used As A Reducing Agent., PDB code: 2bfl:
Jump to Zinc binding site number: 1; 2; 3; 4;

Zinc binding site 1 out of 4 in 2bfl

Go back to Zinc Binding Sites List in 2bfl
Zinc binding site 1 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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:Zn1296

b:29.6
occ:1.00
 ND1 A:HIS118 2.0 23.1 1.0
NE2 A:HIS196 2.1 15.4 1.0
O A:HOH2236 2.1 30.0 1.0
NE2 A:HIS116 2.2 21.8 1.0
O A:HOH2235 2.8 46.7 1.0
CD2 A:HIS196 2.9 15.3 1.0
CG A:HIS118 3.0 24.4 1.0
CE1 A:HIS118 3.0 24.9 1.0
CD2 A:HIS116 3.0 20.4 1.0
CE1 A:HIS196 3.2 15.4 1.0
CE1 A:HIS116 3.3 22.9 1.0
CB A:HIS118 3.3 22.5 1.0
OD1 A:ASP120 4.0 34.1 1.0
NE2 A:HIS118 4.1 25.0 1.0
CD2 A:HIS118 4.1 23.6 1.0
SG A:CYS221 4.1 38.7 1.0
CG A:HIS196 4.1 14.2 1.0
ND1 A:HIS196 4.2 14.7 1.0
CG A:HIS116 4.2 19.5 1.0
ZN A:ZN1297 4.2 82.2 1.0
CB A:CYS221 4.3 23.6 1.0
ND1 A:HIS116 4.3 21.4 1.0
CG2 A:THR197 4.3 15.2 1.0
O A:HOH2099 4.5 49.9 1.0
CA A:HIS118 4.8 23.4 1.0
CG A:ASP120 4.8 33.8 1.0
OD2 A:ASP120 4.8 36.1 1.0
O A:HOH2184 5.0 16.5 1.0

Zinc binding site 2 out of 4 in 2bfl

Go back to Zinc Binding Sites List in 2bfl
Zinc binding site 2 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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:Zn1297

b:82.2
occ:1.00
 SG A:CYS221 2.2 38.7 1.0
O A:HOH2237 2.3 37.5 1.0
O A:HOH2238 2.4 36.5 1.0
NE2 A:HIS263 2.5 32.7 1.0
O A:HOH2236 3.0 30.0 1.0
CD2 A:HIS263 3.0 30.7 1.0
CB A:CYS221 3.1 23.6 1.0
CE1 A:HIS263 3.7 29.9 1.0
O A:HOH2099 3.8 49.9 1.0
OD2 A:ASP120 3.9 36.1 1.0
O A:HOH2185 4.0 26.5 1.0
NE2 A:HIS196 4.1 15.4 1.0
CA A:CYS221 4.1 18.7 1.0
CE1 A:HIS196 4.2 15.4 1.0
ZN A:ZN1296 4.2 29.6 1.0
O A:HOH2235 4.3 46.7 1.0
CG A:HIS263 4.3 27.3 1.0
ND1 A:HIS263 4.6 30.9 1.0
NZ A:LYS224 4.6 29.7 1.0
CG A:ASP120 4.8 33.8 1.0
O A:HOH2029 4.8 45.9 1.0
CD2 A:HIS196 4.9 15.3 1.0
ND1 A:HIS196 4.9 14.7 1.0
O A:HOH2176 5.0 66.1 1.0
N A:CYS221 5.0 16.4 1.0

Zinc binding site 3 out of 4 in 2bfl

Go back to Zinc Binding Sites List in 2bfl
Zinc binding site 3 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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:Zn1298

b:24.5
occ:1.00
 O B:HOH2244 2.0 28.1 1.0
ND1 B:HIS118 2.1 23.4 1.0
NE2 B:HIS196 2.1 15.3 1.0
NE2 B:HIS116 2.2 22.3 1.0
O B:HOH2241 2.9 31.0 1.0
CD2 B:HIS196 2.9 14.6 1.0
CG B:HIS118 3.0 22.1 1.0
CE1 B:HIS118 3.1 22.2 1.0
CD2 B:HIS116 3.1 21.4 1.0
CE1 B:HIS196 3.2 15.1 1.0
CB B:HIS118 3.3 20.7 1.0
CE1 B:HIS116 3.3 22.8 1.0
OD1 B:ASP120 4.0 33.8 1.0
SG B:CYS221 4.0 35.1 1.0
CD2 B:HIS118 4.1 22.2 1.0
NE2 B:HIS118 4.1 23.7 1.0
CG B:HIS196 4.2 14.0 1.0
ZN B:ZN1299 4.2 0.6 1.0
ND1 B:HIS196 4.3 15.3 1.0
CB B:CYS221 4.3 23.7 1.0
CG B:HIS116 4.3 19.4 1.0
ND1 B:HIS116 4.4 20.1 1.0
CG2 B:THR197 4.4 13.9 1.0
OD2 B:ASP120 4.6 34.6 1.0
CG B:ASP120 4.7 31.4 1.0
CA B:HIS118 4.8 20.2 1.0
O B:HOH2190 4.9 44.6 1.0
N1 B:AZI1295 5.0 33.8 1.0

Zinc binding site 4 out of 4 in 2bfl

Go back to Zinc Binding Sites List in 2bfl
Zinc binding site 4 out of 4 in the Bacillus Cereus Metallo-Beta-Lactamase (Bcii) Arg (121) Cys Mutant. Solved at PH5 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 PH5 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:0.6
occ:1.00
 SG B:CYS221 2.2 35.1 1.0
NE2 B:HIS263 2.2 33.6 1.0
O B:HOH2245 2.6 41.8 1.0
N1 B:AZI1295 2.8 33.8 1.0
O B:HOH2244 2.8 28.1 1.0
CD2 B:HIS263 3.2 30.8 1.0
CE1 B:HIS263 3.2 31.6 1.0
CB B:CYS221 3.2 23.7 1.0
OD2 B:ASP120 3.4 34.6 1.0
N2 B:AZI1295 3.4 34.4 1.0
O B:HOH2241 4.1 31.0 1.0
ZN B:ZN1298 4.2 24.5 1.0
N3 B:AZI1295 4.3 34.0 1.0
NE2 B:HIS196 4.3 15.3 1.0
CA B:CYS221 4.3 18.7 1.0
CE1 B:HIS196 4.3 15.1 1.0
ND1 B:HIS263 4.3 30.6 1.0
CG B:HIS263 4.4 28.4 1.0
CG B:ASP120 4.4 31.4 1.0
O B:HOH2045 4.5 47.2 1.0
OD1 B:ASP120 4.8 33.8 1.0
O B:HOH2179 4.9 51.7 1.0
NZ B:LYS224 5.0 18.0 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 21:59:55 2024

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