Potassium in PDB 8riu: Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum

Enzymatic activity of Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum

All present enzymatic activity of Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum:
1.2.7.4;

Protein crystallography data

The structure of Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum, PDB code: 8riu was solved by O.N.Lemaire, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 39.80 / 1.89
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 97.07, 159.213, 191.444, 90, 90, 90
R / Rfree (%) 16.5 / 18.7

Other elements in 8riu:

The structure of Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum also contains other interesting chemical elements:

Chlorine (Cl) 1 atom
Nickel (Ni) 2 atoms
Iron (Fe) 60 atoms

Potassium Binding Sites:

The binding sites of Potassium atom in the Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum (pdb code 8riu). This binding sites where shown within 5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum, PDB code: 8riu:
Jump to Potassium binding site number: 1; 2;

Potassium binding site 1 out of 2 in 8riu

Go back to Potassium Binding Sites List in 8riu
Potassium binding site 1 out of 2 in the Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 1 of Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
A:K821

b:35.3
occ:1.00
 O A:CYS412 2.7 29.5 1.0
O C:PHE5 2.7 27.5 1.0
OD1 C:ASP6 2.8 30.2 1.0
O A:VAL409 2.9 28.3 1.0
O A:HOH1210 3.0 29.0 1.0
O A:ILE410 3.2 36.0 1.0
CD2 C:PHE5 3.5 28.9 1.0
O C:HOH302 3.5 28.0 1.0
C C:PHE5 3.6 32.4 1.0
CE2 C:PHE5 3.6 32.4 1.0
C A:ILE410 3.7 30.1 1.0
CG C:ASP6 3.7 34.6 1.0
CA A:GLY415 3.8 27.7 1.0
CA A:ILE410 3.8 29.7 1.0
C A:CYS412 3.8 29.5 1.0
N A:GLY415 3.9 30.9 1.0
C A:VAL409 4.0 27.6 1.0
CA C:ASP6 4.1 27.9 1.0
CG C:PHE5 4.1 29.1 1.0
N C:ASP6 4.2 29.8 1.0
N A:CYS412 4.2 31.5 1.0
N A:ILE410 4.4 27.3 1.0
CZ C:PHE5 4.4 33.2 1.0
CB C:ASP6 4.5 26.2 1.0
OD2 C:ASP6 4.6 32.1 1.0
CA A:CYS412 4.6 31.4 1.0
CA C:PHE5 4.7 30.1 1.0
N A:ALA411 4.7 33.5 1.0
CB C:PHE5 4.7 33.1 1.0
C A:PRO413 4.8 30.3 1.0
CD1 C:PHE5 4.8 30.4 1.0
O A:PRO413 4.8 32.5 1.0
N A:PRO413 4.8 30.4 1.0
C A:ALA411 4.8 30.1 1.0
CA A:PRO413 4.9 28.7 1.0
CE1 C:PHE5 4.9 29.6 1.0
CB A:CYS412 5.0 29.7 1.0
C A:GLN414 5.0 30.1 1.0

Potassium binding site 2 out of 2 in 8riu

Go back to Potassium Binding Sites List in 8riu
Potassium binding site 2 out of 2 in the Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum


Mono view


Stereo pair view

A full contact list of Potassium with other atoms in the K binding site number 2 of Crystal Structure of the F420-Reducing Carbon Monoxide Dehydrogenase Component From the Ethanotroph Candidatus Ethanoperedens Thermophilum within 5.0Å range:
probe atom residue distance (Å) B Occ
D:K809

b:36.2
occ:1.00
 O F:PHE5 2.6 33.9 1.0
OD1 F:ASP6 2.7 34.7 1.0
O D:CYS412 2.7 34.4 1.0
O F:HOH601 2.9 30.5 1.0
O D:VAL409 2.9 33.8 1.0
O D:ILE410 3.2 32.4 1.0
CD2 F:PHE5 3.4 32.9 1.0
C F:PHE5 3.6 32.5 1.0
CE2 F:PHE5 3.6 35.8 1.0
O D:HOH1006 3.6 31.5 1.0
C D:ILE410 3.7 34.3 1.0
CA D:ILE410 3.7 30.8 1.0
CA D:GLY415 3.8 35.8 1.0
CG F:ASP6 3.8 35.0 1.0
C D:CYS412 3.9 34.0 1.0
N D:GLY415 3.9 30.7 1.0
C D:VAL409 4.0 31.6 1.0
CG F:PHE5 4.0 32.5 1.0
CA F:ASP6 4.1 28.4 1.0
N F:ASP6 4.2 30.0 1.0
N D:CYS412 4.2 32.0 1.0
CZ F:PHE5 4.3 32.4 1.0
N D:ILE410 4.3 36.0 1.0
CA F:PHE5 4.6 29.8 1.0
CA D:CYS412 4.6 32.2 1.0
CB F:ASP6 4.6 27.6 1.0
CB F:PHE5 4.6 34.8 1.0
N D:ALA411 4.6 31.6 1.0
CD1 F:PHE5 4.7 33.6 1.0
OD2 F:ASP6 4.7 30.5 1.0
CE1 F:PHE5 4.8 32.3 1.0
C D:ALA411 4.9 28.8 1.0
N D:PRO413 4.9 31.1 1.0
C D:PRO413 4.9 32.6 1.0
CB D:CYS412 4.9 35.3 1.0
CA D:PRO413 4.9 31.9 1.0
C D:GLN414 5.0 35.4 1.0

Reference:

O.N.Lemaire, G.Wegener, T.Wagner. F420 Reduction As A Cellular Driver For Anaerobic Ethanotrophy To Be Published.
Page generated: Thu Oct 31 21:34:19 2024

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