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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2bs4:

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

Iron (Fe) 22 atoms

Sodium Binding Sites:

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 2bs4

Go back to Sodium Binding Sites List in 2bs4
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 2bs4

Go back to Sodium Binding Sites List in 2bs4
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

Reference:

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
Page generated: Tue Dec 15 05:46:18 2020

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