Sodium in PDB 2bs4: Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes

All present enzymatic activity of Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes:
1.3.99.1;

The structure of Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes, PDB code: 2bs4 was solved by C.R.D.Lancaster, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.65 / 2.76
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	85.104, 188.766, 117.817, 90.00, 104.47, 90.00
R / Rfree (%)	20 / 21.6

The structure of Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes also contains other interesting chemical elements:

Iron

(Fe)

22 atoms

The binding sites of Sodium atom in the Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes (pdb code 2bs4). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes, PDB code: 2bs4:
Jump to Sodium binding site number: 1; 2;

Sodium binding site 1 out of 2 in the Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range: probe atom residue distance (Å) B Occ D:Na1658 b:17.1 occ:1.00 O D:ALA395 2.4 25.1 1.0 O D:GLY373 2.5 24.8 1.0 O D:HOH2083 2.5 25.4 1.0 O D:GLU393 2.6 22.6 1.0 O D:SER371 2.6 27.2 1.0 O D:MET372 2.7 24.7 1.0 C D:MET372 3.2 24.9 1.0 C D:GLU393 3.4 20.9 1.0 C D:GLY373 3.5 24.8 1.0 C D:ALA395 3.6 26.2 1.0 C D:SER371 3.7 25.8 1.0 CA D:MET372 3.8 25.5 1.0 CA D:GLU393 3.8 20.1 1.0 N D:GLY373 3.9 24.2 1.0 OH D:TYR370 4.0 21.2 1.0 N D:ALA395 4.1 24.0 1.0 N D:MET372 4.2 26.1 1.0 CA D:GLY373 4.2 23.9 1.0 O D:HOH2091 4.3 32.9 1.0 CG D:GLU393 4.3 18.6 1.0 O D:GLY392 4.3 18.3 1.0 N D:GLY374 4.4 23.9 1.0 CA D:ALA395 4.4 24.5 1.0 N D:ALA394 4.5 21.0 1.0 C D:ALA394 4.5 21.2 1.0 CA D:GLY374 4.5 23.6 1.0 CZ D:TYR370 4.6 20.4 1.0 O D:HOH2092 4.6 23.4 1.0 N D:CYS396 4.6 28.5 1.0 CB D:GLU393 4.7 19.6 1.0 CE2 D:TYR370 4.7 21.5 1.0 CA D:CYS396 4.8 30.0 1.0 CA D:ALA394 4.9 20.6 1.0 N D:GLU393 4.9 18.6 1.0 O D:HOH2095 4.9 26.6 1.0 CB D:SER371 4.9 23.8 1.0 CA D:SER371 4.9 24.5 1.0

Sodium binding site 2 out of 2 in the Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Glu C180 -> Ile Variant Quinol:Fumarate Reductase From Wolinella Succinogenes within 5.0Å range: probe atom residue distance (Å) B Occ E:Na1243 b:17.1 occ:1.00 O A:ALA395 2.4 25.1 1.0 O A:GLY373 2.5 24.8 1.0 O A:HOH2082 2.5 25.4 1.0 O A:GLU393 2.6 22.6 1.0 O A:SER371 2.6 27.2 1.0 O A:MET372 2.7 24.7 1.0 C A:MET372 3.2 24.9 1.0 C A:GLU393 3.4 20.9 1.0 C A:GLY373 3.5 24.8 1.0 C A:ALA395 3.6 26.2 1.0 C A:SER371 3.7 25.8 1.0 CA A:MET372 3.8 25.5 1.0 CA A:GLU393 3.8 20.1 1.0 N A:GLY373 3.9 24.2 1.0 OH A:TYR370 4.0 21.2 1.0 N A:ALA395 4.1 24.0 1.0 N A:MET372 4.2 26.1 1.0 CA A:GLY373 4.2 23.9 1.0 O A:HOH2090 4.3 32.9 1.0 CG A:GLU393 4.3 18.6 1.0 O A:GLY392 4.3 18.3 1.0 N A:GLY374 4.4 23.9 1.0 CA A:ALA395 4.4 24.5 1.0 N A:ALA394 4.5 21.0 1.0 C A:ALA394 4.5 21.2 1.0 CA A:GLY374 4.5 23.6 1.0 CZ A:TYR370 4.6 20.4 1.0 O A:HOH2091 4.6 23.4 1.0 N A:CYS396 4.6 28.5 1.0 CB A:GLU393 4.7 19.6 1.0 CE2 A:TYR370 4.7 21.5 1.0 CA A:CYS396 4.8 30.0 1.0 CA A:ALA394 4.9 20.6 1.0 N A:GLU393 4.9 18.6 1.0 O A:HOH2095 4.9 26.6 1.0 CB A:SER371 4.9 23.8 1.0 CA A:SER371 4.9 24.5 1.0

C.R.D.Lancaster, U.S.Sauer, R.Gross, A.H.Haas, J.Graf, H.Schwalbe, W.Maentele, J.Simon, G.Madej. Experimental Support For the E-Pathway Hypothesis of Coupled Transmembrane Electron and Proton Transfer in Dihemic Quinol:Fumarate Reductase Proc.Natl.Acad.Sci.Usa V. 102 18860 2005.
ISSN: ISSN 0027-8424
PubMed: 16380425
DOI: 10.1073/PNAS.0509711102