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Caesium in PDB 3ws2: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C)
Enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C)
All present enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C):
3.5.2.6;
3.5.2.6;
Protein crystallography data
The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C), PDB code: 3ws2
was solved by
S.Arai,
Y.Yonezawa,
N.Okazaki,
F.Matsumoto,
R.Shimizu,
M.Yamada,
M.Adachi,
T.Tamada,
H.Tokunaga,
M.Ishibashi,
M.Tokunaga,
R.Kuroki,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 7.50 / 2.10 |
| Space group | P 31 |
| Cell size a, b, c (Å), α, β, γ (°) | 115.308, 115.308, 67.475, 90.00, 90.00, 120.00 |
| R / Rfree (%) | 14.4 / 17.4 |
Other elements in 3ws2:
The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C) also contains other interesting chemical elements:
| Calcium | (Ca) | 10 atoms |
Caesium Binding Sites:
The binding sites of Caesium atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C)
(pdb code 3ws2). This binding sites where shown within
5.0 Angstroms radius around Caesium atom.
In total only one binding site of Caesium was determined in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C), PDB code: 3ws2:
In total only one binding site of Caesium was determined in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C), PDB code: 3ws2:
Caesium binding site 1 out of 1 in 3ws2
Go back to
Caesium Binding Sites List in 3ws2
Caesium binding site 1 out
of 1 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C)
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Caesium with other atoms in the Cs binding
site number 1 of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1C) within 5.0Å range:
|
Reference:
S.Arai,
Y.Yonezawa,
N.Okazaki,
F.Matsumoto,
C.Shibazaki,
R.Shimizu,
M.Yamada,
M.Adachi,
T.Tamada,
T.Kawamoto,
H.Tokunaga,
M.Ishibashi,
M.Blaber,
M.Tokunaga,
R.Kuroki.
Crystal Structure of Highly Acidic Beta-Lactamase From Moderate Halophile Chromohalobacter Sp. 560 and the Discovery of A Cs+ Selective Binding Site To Be Published.
Page generated: Tue Jul 30 20:27:10 2024
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