Magnesium in PDB 7ut9: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/Atp-Bound) During Catalytic N2 Reduction

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

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

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

The binding sites of Magnesium atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/Atp-Bound) During Catalytic N2 Reduction (pdb code 7ut9). 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, Adp/Atp-Bound) During Catalytic N2 Reduction, PDB code: 7ut9:
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, Adp/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, Adp/Atp-Bound) During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg301 b:40.1 occ:1.00 OG E:SER16 2.2 46.5 1.0 O2B E:ADP302 2.3 47.5 1.0 OD2 E:ASP39 2.7 56.7 1.0 PB E:ADP302 3.4 49.5 1.0 O1B E:ADP302 3.6 54.1 1.0 CB E:SER16 3.6 47.6 1.0 OD1 E:ASP125 3.9 48.8 1.0 CG E:ASP39 4.0 56.4 1.0 OD2 E:ASP125 4.0 50.1 1.0 N E:SER16 4.1 44.8 1.0 OD1 E:ASP43 4.2 52.5 1.0 CG E:ASP125 4.3 47.3 1.0 CE E:LYS15 4.4 40.8 1.0 CA E:SER16 4.4 43.1 1.0 O3A E:ADP302 4.4 51.7 1.0 O3B E:ADP302 4.5 56.7 1.0 O E:VAL126 4.6 44.7 1.0 CB E:LYS15 4.6 37.6 1.0 CG E:ASP43 4.7 51.4 1.0 CB E:ASP39 4.8 56.8 1.0 O2A E:ADP302 4.8 57.2 1.0 OD1 E:ASP39 4.8 55.6 1.0 NZ E:LYS15 4.8 48.6 1.0 OD2 E:ASP43 4.9 50.7 1.0 OG E:SER44 5.0 50.5 1.0

Magnesium binding site 2 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (1:1 Fep:Mofep, Adp/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, Adp/Atp-Bound) During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg302 b:53.6 occ:1.00 O1B F:ATP303 2.3 65.3 1.0 OG F:SER16 2.3 53.5 1.0 O3G F:ATP303 2.6 71.4 1.0 O2G F:ATP303 3.3 69.9 1.0 OD2 F:ASP39 3.3 55.7 1.0 PG F:ATP303 3.3 84.5 1.0 PB F:ATP303 3.4 64.2 1.0 CB F:SER16 3.4 55.5 1.0 O3B F:ATP303 3.6 69.5 1.0 OD1 F:ASP125 3.9 50.1 1.0 N F:SER16 3.9 52.9 1.0 OD2 F:ASP125 3.9 51.5 1.0 CA F:SER16 4.1 54.1 1.0 O F:VAL126 4.2 46.6 1.0 O2B F:ATP303 4.2 67.7 1.0 CG F:ASP125 4.3 50.8 1.0 CG F:ASP39 4.4 53.8 1.0 CE F:LYS15 4.5 51.9 1.0 O3A F:ATP303 4.6 60.0 1.0 O1A F:ATP303 4.6 67.5 1.0 CB F:LYS15 4.7 52.4 1.0 NZ F:LYS15 4.8 53.9 1.0 O1G F:ATP303 4.8 69.8 1.0 CB F:ASP39 4.9 51.2 1.0 OG F:SER44 4.9 45.7 1.0 C F:LYS15 4.9 49.4 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