Atomistry » Caesium » PDB 2ov4-4ht3 » 3ws2
Atomistry »
  Caesium »
    PDB 2ov4-4ht3 »
      3ws2 »

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

Last articles

Zn in 7VD8
Zn in 7V1R
Zn in 7V1Q
Zn in 7VPF
Zn in 7T85
Zn in 7T5F
Zn in 7NF9
Zn in 7M4M
Zn in 7M4O
Zn in 7M4N
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy