Sodium in PDB 6v6g: Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase

Enzymatic activity of Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase

All present enzymatic activity of Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase:
3.5.2.6;

Protein crystallography data

The structure of Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase, PDB code: 6v6g was solved by C.A.Brown, L.Hu, B.V.V.Prasad, T.G.Palzkill, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 35.88 / 1.50
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 41.428, 41.428, 231.066, 90.00, 90.00, 120.00
R / Rfree (%) 18.3 / 21.7

Sodium Binding Sites:

The binding sites of Sodium atom in the Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase (pdb code 6v6g). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase, PDB code: 6v6g:

Sodium binding site 1 out of 1 in 6v6g

Go back to Sodium Binding Sites List in 6v6g
Sodium binding site 1 out of 1 in the Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Crystal Structure of Ctx-M-14 E166A/P167S/D240G Beta-Lactamase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na302

b:29.4
occ:1.00
O A:THR171 2.5 16.3 1.0
O A:HOH638 2.7 24.9 1.0
NE2 A:GLN270 2.9 27.2 1.0
C A:THR171 3.4 16.0 1.0
CA A:THR171 3.6 13.4 1.0
CA A:GLY240 3.8 10.9 1.0
CE2 A:TYR241 3.8 14.1 1.0
CD A:GLN270 3.9 28.6 1.0
CB A:THR171 3.9 11.7 1.0
CD2 A:TYR241 3.9 15.3 1.0
CG A:GLN270 3.9 23.0 1.0
CG1 A:ILE173 4.4 14.3 1.0
C A:GLY240 4.5 12.1 1.0
N A:GLY240 4.5 11.8 1.0
N A:ALA172 4.6 12.6 1.0
N A:TYR241 4.6 13.8 1.0
CG2 A:THR171 4.6 16.8 1.0
O A:HOH487 4.8 20.9 1.0
O A:HOH587 5.0 36.0 1.0

Reference:

C.A.Brown, L.Hu, Z.Sun, M.P.Patel, S.Singh, J.R.Porter, B.Sankaran, B.V.V.Prasad, G.R.Bowman, T.G.Palzkill. Antagonism Between Substitutions in Beta-Lactamase Explains A Path Not Taken in the Evolution of Bacterial Drug Resistance J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
Page generated: Tue Dec 15 14:44:09 2020

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