Magnesium in PDB 7ut8: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction:
1.18.6.1;

The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction also contains other interesting chemical elements:

Iron	(Fe)	36 atoms
Molybdenum	(Mo)	2 atoms

The binding sites of Magnesium atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction (pdb code 7ut8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction, PDB code: 7ut8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg302 b:40.9 occ:1.00 OG E:SER16 2.4 42.8 1.0 O2B E:ATP303 2.4 45.3 1.0 O1G E:ATP303 2.7 46.0 1.0 O3B E:ATP303 2.8 45.9 1.0 PB E:ATP303 3.2 27.3 1.0 OD2 E:ASP39 3.2 51.7 1.0 PG E:ATP303 3.4 54.0 1.0 OD1 E:ASP43 3.5 54.1 1.0 CB E:SER16 3.7 43.2 1.0 NZ E:LYS41 4.0 47.6 1.0 OD2 E:ASP125 4.1 45.9 1.0 OD1 E:ASP125 4.1 44.6 1.0 N E:SER16 4.2 36.7 1.0 O2G E:ATP303 4.3 47.4 1.0 O1B E:ATP303 4.3 45.8 1.0 O3A E:ATP303 4.3 31.4 1.0 CE E:LYS15 4.3 43.2 1.0 CG E:ASP43 4.3 55.4 1.0 CG E:ASP39 4.4 51.6 1.0 OD2 E:ASP43 4.4 55.2 1.0 O3G E:ATP303 4.5 48.6 1.0 CA E:SER16 4.5 38.1 1.0 CG E:ASP125 4.6 45.7 1.0 CB E:LYS15 4.6 38.5 1.0 O2A E:ATP303 4.8 47.0 1.0 CB E:ASP39 4.8 48.4 1.0 O E:VAL126 4.8 42.0 1.0 NZ E:LYS15 4.9 44.6 1.0 PA E:ATP303 4.9 31.2 1.0 O1A E:ATP303 5.0 46.4 1.0

Magnesium binding site 2 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Atp-Bound) During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg301 b:39.5 occ:1.00 O1B F:ATP302 2.4 49.0 1.0 OG F:SER16 2.4 39.0 1.0 O3G F:ATP302 2.5 52.0 1.0 CB F:SER16 3.5 39.3 1.0 PG F:ATP302 3.6 55.6 1.0 PB F:ATP302 3.6 40.5 1.0 O1A F:ATP302 3.6 52.8 1.0 O3B F:ATP302 3.8 50.8 1.0 OD2 F:ASP39 4.0 48.0 1.0 O2G F:ATP302 4.0 53.1 1.0 N F:SER16 4.3 38.7 1.0 OD1 F:ASP125 4.4 43.1 1.0 O3A F:ATP302 4.5 42.5 1.0 PA F:ATP302 4.5 41.4 1.0 CA F:SER16 4.5 37.7 1.0 NZ F:LYS41 4.5 49.3 1.0 OD1 F:ASP43 4.7 50.1 1.0 OD2 F:ASP125 4.7 44.5 1.0 O2A F:ATP302 4.8 50.3 1.0 O2B F:ATP302 4.8 53.8 1.0 OD2 F:ASP43 4.9 51.6 1.0 O1G F:ATP302 4.9 52.8 1.0 CG F:ASP39 4.9 47.2 1.0 CG F:ASP125 5.0 42.7 1.0 CG F:ASP43 5.0 50.9 1.0

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641