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
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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
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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
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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
|