Potassium in PDB 4xra: Salmonella Typhimurium Ahpc T43S Mutant

All present enzymatic activity of Salmonella Typhimurium Ahpc T43S Mutant:
1.11.1.15;

The structure of Salmonella Typhimurium Ahpc T43S Mutant, PDB code: 4xra was solved by A.Perkins, A.E.Brereton, K.Nelson, D.Parsonage, L.Poole, P.A.Karplus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	36.28 / 1.75
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	127.069, 171.920, 135.290, 90.00, 90.00, 90.00
R / Rfree (%)	17.1 / 20

The structure of Salmonella Typhimurium Ahpc T43S Mutant also contains other interesting chemical elements:

Chlorine

(Cl)

11 atoms

The binding sites of Potassium atom in the Salmonella Typhimurium Ahpc T43S Mutant (pdb code 4xra). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 3 binding sites of Potassium where determined in the Salmonella Typhimurium Ahpc T43S Mutant, PDB code: 4xra:
Jump to Potassium binding site number: 1; 2; 3;

Potassium binding site 1 out of 3 in the Salmonella Typhimurium Ahpc T43S Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Salmonella Typhimurium Ahpc T43S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:K204 b:52.0 occ:0.50 O A:THR72 2.9 24.9 1.0 O A:HOH312 2.9 28.0 1.0 O A:HOH306 3.1 27.5 1.0 HA A:ASP73 3.6 30.9 1.0 HA A:PRO99 3.6 31.3 1.0 HB A:THR72 3.7 31.9 1.0 C A:THR72 3.8 23.7 1.0 HB3 A:PRO99 3.9 32.2 1.0 OG1 A:THR72 4.3 25.5 1.0 CB A:THR72 4.4 26.6 1.0 CA A:ASP73 4.4 25.8 1.0 N A:ASP73 4.4 25.6 1.0 HG1 A:THR72 4.4 30.6 1.0 CA A:PRO99 4.5 26.1 1.0 CB A:PRO99 4.6 26.9 1.0 O A:PRO99 4.8 26.5 1.0 CA A:THR72 4.8 25.0 1.0 HB2 A:PRO99 4.8 32.2 1.0 O A:HOH301 4.9 29.5 1.0 HG23 A:THR74 5.0 29.0 1.0

Potassium binding site 2 out of 3 in the Salmonella Typhimurium Ahpc T43S Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Salmonella Typhimurium Ahpc T43S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:K203 b:52.2 occ:1.00 O C:THR72 2.8 26.8 1.0 O B:THR72 2.9 24.8 1.0 O B:HOH345 2.9 27.7 1.0 O C:HOH319 2.9 27.7 1.0 O B:HOH351 3.1 29.5 1.0 O C:HOH322 3.1 28.4 1.0 HA C:PRO99 3.5 28.4 1.0 HA B:PRO99 3.5 31.4 1.0 HA C:ASP73 3.6 32.2 1.0 HA B:ASP73 3.6 27.6 1.0 C C:THR72 3.7 27.5 1.0 HB3 C:PRO99 3.7 29.1 1.0 HB C:THR72 3.8 29.6 1.0 HB B:THR72 3.8 24.8 1.0 HB3 B:PRO99 3.8 33.8 1.0 C B:THR72 3.8 25.7 1.0 OG1 C:THR72 4.3 25.3 1.0 CA C:PRO99 4.3 23.7 1.0 CB C:PRO99 4.3 24.2 1.0 CA B:PRO99 4.4 26.1 1.0 CA C:ASP73 4.4 26.9 1.0 CA B:ASP73 4.4 23.0 1.0 CB C:THR72 4.4 24.6 1.0 OG1 B:THR72 4.4 22.9 1.0 N C:ASP73 4.4 24.4 1.0 HG1 C:THR72 4.4 30.3 1.0 N B:ASP73 4.4 25.1 1.0 CB B:THR72 4.4 20.6 1.0 CB B:PRO99 4.5 28.2 1.0 HB2 C:PRO99 4.5 29.1 1.0 HG1 B:THR72 4.5 27.4 1.0 HB2 B:PRO99 4.7 33.8 1.0 CA C:THR72 4.7 24.7 1.0 O C:PRO99 4.8 24.8 1.0 O B:PRO99 4.8 24.8 1.0 CA B:THR72 4.8 24.1 1.0 HG23 C:THR74 4.9 31.1 1.0 O B:HOH343 4.9 30.0 1.0 HG23 B:THR74 4.9 30.4 1.0 O C:HOH317 4.9 28.9 1.0

Potassium binding site 3 out of 3 in the Salmonella Typhimurium Ahpc T43S Mutant


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 3 of Salmonella Typhimurium Ahpc T43S Mutant within 5.0Å range: probe atom residue distance (Å) B Occ D:K203 b:60.4 occ:1.00 O E:THR72 2.8 31.4 1.0 O D:THR72 2.8 30.2 1.0 O E:HOH337 2.9 34.4 1.0 O D:HOH336 2.9 33.9 1.0 O E:HOH336 3.0 35.1 1.0 O D:HOH418 3.1 35.5 1.0 HA E:PRO99 3.5 38.1 1.0 HA E:ASP73 3.5 39.2 1.0 HA D:ASP73 3.5 37.6 1.0 HA D:PRO99 3.6 36.9 1.0 C E:THR72 3.8 33.3 1.0 HB D:THR72 3.8 35.5 1.0 C D:THR72 3.8 31.7 1.0 HB3 D:PRO99 3.8 34.1 1.0 HB3 E:PRO99 3.8 39.4 1.0 HB E:THR72 3.9 36.8 1.0 OG1 E:THR72 4.3 29.3 1.0 OG1 D:THR72 4.3 31.5 1.0 CA E:ASP73 4.3 32.7 1.0 CA E:PRO99 4.3 31.8 1.0 CA D:ASP73 4.4 31.4 1.0 N D:ASP73 4.4 30.8 1.0 N E:ASP73 4.4 30.9 1.0 CB D:THR72 4.4 29.6 1.0 CA D:PRO99 4.4 30.8 1.0 HG1 D:THR72 4.4 37.8 1.0 HG1 E:THR72 4.4 35.2 1.0 CB D:PRO99 4.5 28.4 1.0 CB E:PRO99 4.5 32.8 1.0 CB E:THR72 4.5 30.7 1.0 HB2 D:PRO99 4.7 34.1 1.0 HB2 E:PRO99 4.7 39.4 1.0 CA E:THR72 4.8 30.0 1.0 CA D:THR72 4.8 29.9 1.0 O E:PRO99 4.8 32.6 1.0 O D:PRO99 4.8 31.5 1.0 HG23 E:THR74 4.8 39.7 1.0 O D:HOH333 4.9 39.5 1.0 HG23 D:THR74 4.9 39.0 1.0 O E:HOH332 4.9 35.9 1.0 C E:ASP73 5.0 37.1 1.0

K.J.Nelson, A.Perkins, A.E.D.Van Swearingen, S.Hartman, A.E.Brereton, D.Parsonage, F.R.Salsbury Jr., P.A.Karplus, L.B.Poole. Experimentally Dissecting the Origins of Peroxiredoxin Catalysis. Antioxid.Redox Signal. V. 28 521 2018.
ISSN: ESSN 1557-7716
PubMed: 28375740
DOI: 10.1089/ARS.2016.6922