Sodium in PDB 7zkj: Codh/Acs Complex of C. Hydrogenoformans

Enzymatic activity of Codh/Acs Complex of C. Hydrogenoformans

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

Protein crystallography data

The structure of Codh/Acs Complex of C. Hydrogenoformans, PDB code: 7zkj 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) 48.35 / 2.04
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 141.586, 141.586, 290.124, 90, 90, 120
R / Rfree (%) 17.4 / 19.9

Other elements in 7zkj:

The structure of 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 Codh/Acs Complex of C. Hydrogenoformans (pdb code 7zkj). 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 Codh/Acs Complex of C. Hydrogenoformans, PDB code: 7zkj:

Sodium binding site 1 out of 1 in 7zkj

Go back to Sodium Binding Sites List in 7zkj
Sodium binding site 1 out of 1 in 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 Codh/Acs Complex of C. Hydrogenoformans within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Na808

b:34.7
occ:1.00
O B:HOH1071 2.3 30.8 1.0
O B:PHE420 2.4 33.8 1.0
O B:ASN415 2.4 34.6 1.0
O B:GLY417 2.5 35.5 1.0
OE1 B:GLU334 2.5 35.7 1.0
O B:PHE331 2.8 37.2 1.0
C B:ASN415 3.3 39.3 1.0
C B:PHE420 3.6 34.2 1.0
CD B:GLU334 3.6 45.0 1.0
C B:GLY417 3.6 36.1 1.0
CB B:GLU334 3.7 37.6 1.0
C B:PHE331 3.7 34.6 1.0
CA B:ASN415 3.7 36.8 1.0
CB B:PHE331 3.8 32.6 1.0
N B:PHE420 4.1 32.7 1.0
CG B:GLU334 4.2 43.8 1.0
N B:GLY417 4.3 33.9 1.0
N B:GLY419 4.3 36.6 1.0
CA B:PHE331 4.4 35.3 1.0
CA B:PHE420 4.4 34.3 1.0
N B:TYR416 4.4 39.6 1.0
CB B:ASN415 4.4 38.5 1.0
C B:TYR416 4.5 40.9 1.0
O B:THR414 4.5 36.8 1.0
CA B:GLY417 4.5 37.7 1.0
OD1 B:ASN415 4.5 38.0 1.0
N B:GLU418 4.5 33.0 1.0
N B:TRP421 4.6 33.0 1.0
CA B:GLU418 4.6 34.2 1.0
N B:GLU332 4.6 36.5 1.0
OE2 B:GLU334 4.7 50.6 1.0
CA B:TRP421 4.7 30.2 1.0
CA B:GLU332 4.8 38.0 1.0
CA B:TYR416 4.8 36.9 1.0
O B:GLU332 4.8 37.7 1.0
CB B:PHE420 4.9 32.3 1.0
C B:GLU418 4.9 37.1 1.0
O B:TYR416 4.9 40.5 1.0
CA B:GLU334 4.9 39.8 1.0
C B:GLU332 4.9 39.4 1.0
N B:ASN415 5.0 33.6 1.0
N B:GLU334 5.0 35.8 1.0
CG B:ASN415 5.0 37.0 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: Fri Apr 7 17:27:07 2023

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