Caesium in PDB 3ws1: N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1B)

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

The structure of N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1B), PDB code: 3ws1 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)	37.68 / 1.80
Space group	P 31
Cell size a, b, c (Å), α, β, γ (°)	115.125, 115.125, 67.317, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 21.1

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

Calcium

(Ca)

10 atoms

The binding sites of Caesium atom in the N288Q-N321Q Mutant Beta-Lactamase Derived From Chromohalobacter Sp.560 (Condition-1B) (pdb code 3ws1). 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-1B), PDB code: 3ws1:
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-1B)


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-1B) within 5.0Å range: probe atom residue distance (Å) B Occ A:Cs401 b:40.2 occ:0.36 NH1 A:ARG176 2.9 38.1 1.0 O A:HOH712 3.1 26.6 1.0 O A:GLN186 3.2 31.2 1.0 CH2 A:TRP189 3.2 27.3 1.0 CZ2 A:TRP189 3.4 26.9 1.0 NH2 A:ARG176 3.4 35.4 1.0 O A:HOH530 3.4 26.3 1.0 CZ3 A:TRP189 3.5 26.3 1.0 O A:THR188 3.5 23.5 1.0 CZ A:ARG176 3.5 36.0 1.0 C A:GLN186 3.7 30.5 1.0 CE2 A:TRP189 3.8 25.2 1.0 CE3 A:TRP189 3.9 24.6 1.0 CD2 A:TRP189 4.0 24.1 1.0 CA A:GLN186 4.0 31.5 1.0 O A:HOH532 4.3 18.1 1.0 OE1 A:GLN186 4.3 41.4 1.0 N A:THR188 4.4 24.3 1.0 C A:THR188 4.5 22.1 1.0 O A:MET185 4.5 24.8 1.0 N A:ASP187 4.6 28.5 1.0 NE1 A:TRP189 4.6 25.1 1.0 NE A:ARG176 4.8 35.1 1.0 CB A:GLN186 4.8 35.0 1.0 CG A:TRP189 4.9 22.9 1.0 CA A:ASP187 5.0 28.3 1.0

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


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-1B) within 5.0Å range: probe atom residue distance (Å) B Occ C:Cs401 b:50.3 occ:0.27 O C:THR188 3.2 18.9 1.0 CZ3 C:TRP189 3.3 26.7 1.0 CH2 C:TRP189 3.4 28.0 1.0 O C:GLN186 3.4 26.8 1.0 CE3 C:TRP189 3.6 24.8 1.0 CZ2 C:TRP189 3.7 26.8 1.0 CD2 C:TRP189 3.8 24.0 1.0 CE2 C:TRP189 3.9 25.2 1.0 C C:GLN186 3.9 26.7 1.0 C C:THR188 4.3 18.9 1.0 CA C:GLN186 4.3 27.6 1.0 N C:THR188 4.5 20.8 1.0 O C:MET185 4.5 21.7 1.0 OE1 C:GLN186 4.6 44.9 1.0 CG C:TRP189 4.8 23.1 1.0 N C:ASP187 4.8 25.4 1.0 NE1 C:TRP189 4.8 25.2 1.0 CD C:ARG176 4.8 30.6 1.0 CA C:THR188 4.9 18.8 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.