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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;

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:

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

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:
probe atom residue distance (Å) B Occ
A:Cs401

b:34.3
occ:0.34
 NH1 A:ARG176 2.9 37.4 1.0
O A:GLN186 3.1 26.4 1.0
O C:HOH533 3.3 34.4 1.0
CH2 A:TRP189 3.3 28.1 1.0
CZ2 A:TRP189 3.4 27.8 1.0
NH2 A:ARG176 3.5 35.2 1.0
CZ A:ARG176 3.6 36.7 1.0
CZ3 A:TRP189 3.6 28.8 1.0
O A:THR188 3.7 24.9 1.0
CE2 A:TRP189 3.7 27.9 1.0
C A:GLN186 3.8 26.4 1.0
CE3 A:TRP189 3.9 26.9 1.0
CD2 A:TRP189 3.9 26.4 1.0
O A:HOH531 4.1 36.8 1.0
CA A:GLN186 4.2 26.8 1.0
OE1 A:GLN186 4.4 37.0 1.0
NE1 A:TRP189 4.5 26.8 1.0
N A:THR188 4.5 26.2 1.0
C A:THR188 4.6 23.8 1.0
N A:ASP187 4.8 24.3 1.0
NE A:ARG176 4.8 35.7 1.0
O A:MET185 4.8 27.7 1.0
CG A:TRP189 4.8 25.7 1.0

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: Sun Dec 13 10:56:14 2020

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