Magnesium in PDB 9cu0: Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry):
1.18.6.1;

The structure of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) also contains other interesting chemical elements:

Molybdenum	(Mo)	2 atoms
Iron	(Fe)	38 atoms

The binding sites of Magnesium atom in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) (pdb code 9cu0). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry), PDB code: 9cu0:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg302 b:221.8 occ:1.00 OG E:SER17 2.1 227.5 1.0 O3B E:ADP301 2.4 230.9 1.0 OD2 E:ASP40 3.0 216.3 1.0 CB E:SER17 3.2 227.5 1.0 PB E:ADP301 3.3 230.9 1.0 O3A E:ADP301 3.3 230.9 1.0 NZ E:LYS42 3.5 217.2 1.0 O1A E:ADP301 3.6 230.9 1.0 O2B E:ADP301 3.7 230.9 1.0 CE E:LYS42 3.7 217.2 1.0 PA E:ADP301 3.9 230.9 1.0 O2A E:ADP301 4.2 230.9 1.0 CG E:ASP40 4.2 216.3 1.0 OG E:SER45 4.2 228.1 1.0 N E:SER17 4.2 227.5 1.0 OD2 E:ASP126 4.3 221.8 1.0 CA E:SER17 4.3 227.5 1.0 CB E:ASP40 4.6 216.3 1.0 O1B E:ADP301 4.7 230.9 1.0 CB E:ASP44 4.7 229.6 1.0 CG E:LYS42 4.8 217.2 1.0 C E:ASP44 4.8 229.6 1.0 O E:ASP44 4.8 229.6 1.0 CD E:LYS42 4.8 217.2 1.0 N E:SER45 4.9 228.1 1.0

Magnesium binding site 2 out of 2 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg303 b:218.9 occ:1.00 O2B F:ADP302 2.1 222.5 1.0 OG F:SER17 2.4 215.3 1.0 OD2 F:ASP40 3.2 209.8 1.0 PB F:ADP302 3.3 222.5 1.0 CB F:SER17 3.3 215.3 1.0 O1B F:ADP302 3.8 222.5 1.0 O3B F:ADP302 4.0 222.5 1.0 CG F:ASP40 4.3 209.8 1.0 O3A F:ADP302 4.6 222.5 1.0 CA F:SER17 4.6 215.3 1.0 O2A F:ADP302 4.6 222.5 1.0 CB F:LYS42 4.8 208.4 1.0 CB F:ASP40 4.9 209.8 1.0 O1A F:ADP302 4.9 222.5 1.0 N F:SER17 4.9 215.3 1.0 PA F:ADP302 4.9 222.5 1.0 CD F:LYS42 5.0 208.4 1.0

S.M.Narehood, B.D.Cook, S.Srisantitham, V.H.Eng, A.Shiau, K.L.Mcguire, R.D.Britt, M.A.Herzik, F.A.Tezcan. Structural Basis For the Conformational Protection of Nitrogenase From O2 Nature 2025.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41586-024-08311-1