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Sodium in PDB 5uka: Salmonella Typhimurium Ahpc E49Q Mutant

Enzymatic activity of Salmonella Typhimurium Ahpc E49Q Mutant

All present enzymatic activity of Salmonella Typhimurium Ahpc E49Q Mutant:
1.11.1.15;

Protein crystallography data

The structure of Salmonella Typhimurium Ahpc E49Q Mutant, PDB code: 5uka was solved by A.Perkins, 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) 27.26 / 1.90
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 126.902, 171.950, 135.766, 90.00, 90.00, 90.00
R / Rfree (%) 17.5 / 21

Other elements in 5uka:

The structure of Salmonella Typhimurium Ahpc E49Q Mutant also contains other interesting chemical elements:

Potassium (K) 3 atoms
Chlorine (Cl) 5 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Salmonella Typhimurium Ahpc E49Q Mutant (pdb code 5uka). 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 Salmonella Typhimurium Ahpc E49Q Mutant, PDB code: 5uka:

Sodium binding site 1 out of 1 in 5uka

Go back to Sodium Binding Sites List in 5uka
Sodium binding site 1 out of 1 in the Salmonella Typhimurium Ahpc E49Q Mutant


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Salmonella Typhimurium Ahpc E49Q Mutant within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na203

b:89.4
occ:1.00
O A:HOH319 2.5 38.2 1.0
O B:HOH363 3.0 51.6 1.0
OD2 B:ASP118 3.3 39.5 1.0
HA B:ARG111 3.4 47.8 1.0
O B:HOH394 3.4 59.0 1.0
O B:HOH395 3.7 51.5 1.0
O B:MET110 3.8 36.2 1.0
HG2 B:ARG111 3.8 82.6 1.0
CA B:ARG111 4.2 39.8 1.0
CG B:ASP118 4.3 34.3 1.0
O A:ILE3 4.3 29.7 1.0
HG22 A:ILE3 4.4 29.1 1.0
O A:SER1 4.4 33.9 1.0
OD1 B:ASP118 4.4 36.3 1.0
CG B:ARG111 4.4 68.9 1.0
HG3 B:ARG111 4.5 82.6 1.0
C B:MET110 4.5 35.8 1.0
HB3 B:ARG111 4.6 56.8 1.0
CB B:ARG111 4.6 47.4 1.0
HG23 A:ILE3 4.7 29.1 1.0
N B:ARG111 4.7 38.5 1.0
H B:GLU112 4.9 44.6 1.0
O A:HOH314 4.9 32.4 1.0
CG2 A:ILE3 5.0 24.3 1.0

Reference:

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
Page generated: Tue Dec 15 11:42:28 2020

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