Caesium in PDB 3ws0: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)

All present enzymatic activity of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A):
3.5.2.6;

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A), PDB code: 3ws0 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)	29.88 / 2.00
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	115.393, 115.393, 67.652, 90.00, 90.00, 120.00
R / Rfree (%)	19 / 22.4

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A) also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Calcium	(Ca)	10 atoms

The binding sites of Caesium atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A) (pdb code 3ws0). This binding sites where shown within 5.0 Angstroms radius around Caesium atom.
In total 2 binding sites of Caesium where determined in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A), PDB code: 3ws0:
Jump to Caesium binding site number: 1; 2;

Caesium binding site 1 out of 2 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)


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-1A) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cs405 b:36.1 occ:1.00 O A:HOH691 3.1 40.5 1.0 O A:GLN186 3.1 32.4 1.0 O C:HOH515 3.1 30.2 1.0 O A:HOH545 3.2 25.3 1.0 CH2 A:TRP189 3.3 29.6 1.0 NH2 A:ARG176 3.4 54.3 1.0 CZ2 A:TRP189 3.5 28.8 1.0 CZ3 A:TRP189 3.5 28.3 1.0 CE2 A:TRP189 3.7 27.3 1.0 O A:THR188 3.7 25.6 1.0 CE3 A:TRP189 3.8 26.9 1.0 C A:GLN186 3.9 31.6 1.0 CD2 A:TRP189 3.9 26.2 1.0 CZ A:ARG176 4.3 50.9 1.0 CA A:GLN186 4.4 32.4 1.0 CD A:ARG176 4.4 43.4 1.0 NE1 A:TRP189 4.5 26.6 1.0 N A:THR188 4.6 25.9 1.0 C A:THR188 4.6 24.6 1.0 NE A:ARG176 4.7 45.9 1.0 N A:ASP187 4.7 29.9 1.0 CG A:TRP189 4.8 25.4 1.0 O A:HOH693 4.8 55.8 1.0 OE1 A:GLN186 4.9 46.1 1.0 CA A:ASP187 5.0 29.5 1.0

Caesium binding site 2 out of 2 in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A)


Mono view


Stereo pair view

A full contact list of Caesium with other atoms in the Cs binding site number 2 of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1A) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cs404 b:62.4 occ:1.00 NH2 C:ARG176 3.2 38.4 1.0 O C:GLN186 3.2 26.9 1.0 O C:THR188 3.3 22.5 1.0 CZ C:ARG176 3.4 37.0 1.0 CH2 C:TRP189 3.4 30.6 1.0 CZ3 C:TRP189 3.4 29.6 1.0 NH1 C:ARG176 3.5 36.5 1.0 CZ2 C:TRP189 3.5 29.6 1.0 CE3 C:TRP189 3.6 27.4 1.0 CE2 C:TRP189 3.6 27.7 1.0 CD2 C:TRP189 3.7 26.2 1.0 C C:GLN186 3.9 26.8 1.0 NE C:ARG176 4.2 36.6 1.0 C C:THR188 4.2 21.5 1.0 N C:THR188 4.3 21.4 1.0 CA C:GLN186 4.4 27.4 1.0 NE1 C:TRP189 4.4 27.6 1.0 CG C:TRP189 4.5 25.1 1.0 N C:ASP187 4.7 24.5 1.0 O C:MET185 4.7 22.6 1.0 CD C:ARG176 4.9 35.3 1.0 OE1 C:GLN186 4.9 37.7 1.0 CD1 C:TRP189 4.9 25.4 1.0 CA C:THR188 4.9 20.6 1.0 CA C:ASP187 4.9 24.6 1.0 C C:ASP187 5.0 22.6 1.0

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.