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Sodium in PDB 7zkv: F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans

Enzymatic activity of F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans

All present enzymatic activity of F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans:
1.2.7.4; 2.3.1.169;

Protein crystallography data

The structure of F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans, PDB code: 7zkv was solved by J.Ruickoldt, J.-H.Jeoung, Y.Basak, L.Domnik, H.Dobbek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.38 / 2.07
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 142.64, 142.64, 291.31, 90, 90, 120
R / Rfree (%) 17.3 / 21.4

Other elements in 7zkv:

The structure of F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans also contains other interesting chemical elements:

Nickel (Ni) 3 atoms
Iron (Fe) 14 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans (pdb code 7zkv). 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 F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans, PDB code: 7zkv:

Sodium binding site 1 out of 1 in 7zkv

Go back to Sodium Binding Sites List in 7zkv
Sodium binding site 1 out of 1 in the F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of F231A Variant of the Codh/Acs Complex of C. Hydrogenoformans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na805

b:31.1
occ:1.00
OE1 B:GLU334 2.4 39.9 1.0
O B:PHE420 2.4 29.5 1.0
O B:ASN415 2.4 31.9 1.0
O B:HOH1108 2.4 27.4 1.0
O B:GLY417 2.4 31.8 1.0
O B:PHE331 2.9 31.7 1.0
C B:ASN415 3.3 38.3 1.0
CD B:GLU334 3.5 44.9 1.0
C B:GLY417 3.6 32.4 1.0
C B:PHE420 3.6 27.1 1.0
CA B:ASN415 3.7 33.0 1.0
CB B:GLU334 3.8 32.2 1.0
C B:PHE331 3.8 33.5 1.0
CB B:PHE331 3.9 32.3 1.0
N B:PHE420 4.1 32.3 1.0
CG B:GLU334 4.2 41.2 1.0
N B:GLY419 4.2 30.2 1.0
N B:GLY417 4.2 31.5 1.0
CA B:PHE420 4.4 33.7 1.0
CB B:ASN415 4.4 31.7 1.0
N B:TYR416 4.4 38.5 1.0
C B:TYR416 4.4 30.1 1.0
N B:GLU418 4.5 28.4 1.0
CA B:PHE331 4.5 32.6 1.0
CA B:GLY417 4.5 30.5 1.0
O B:THR414 4.5 34.0 1.0
OD1 B:ASN415 4.5 36.2 1.0
CA B:GLU418 4.5 30.1 1.0
OE2 B:GLU334 4.6 50.3 1.0
N B:TRP421 4.6 30.6 1.0
N B:GLU332 4.7 32.2 1.0
CA B:TRP421 4.7 27.8 1.0
CB B:PHE420 4.8 32.1 1.0
CA B:GLU332 4.8 34.6 1.0
C B:GLU418 4.8 32.2 1.0
CA B:TYR416 4.8 31.6 1.0
O B:TYR416 4.9 36.4 1.0
O B:GLU332 4.9 34.8 1.0
N B:ASN415 4.9 26.6 1.0
C B:GLY419 5.0 33.3 1.0
CG B:ASN415 5.0 34.3 1.0

Reference:

J.Ruickoldt, Y.Basak, L.Domnik, J.H.Jeoung, H.Dobbek. On the Kinetics of CO2 Reduction By Ni, Fe-Co Dehydrogenases Acs Catal. 2022.
DOI: 10.1021/ACSCATAL.2C02221
Page generated: Wed Oct 9 10:17:19 2024

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