Magnesium in PDB 8oie: Iron Nitrogenase Complex From Rhodobacter Capsulatus

All present enzymatic activity of Iron Nitrogenase Complex From Rhodobacter Capsulatus:
1.18.6.1;

The structure of Iron Nitrogenase Complex From Rhodobacter Capsulatus also contains other interesting chemical elements:

Aluminium	(Al)	4 atoms
Iron	(Fe)	40 atoms
Fluorine	(F)	12 atoms

The binding sites of Magnesium atom in the Iron Nitrogenase Complex From Rhodobacter Capsulatus (pdb code 8oie). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Iron Nitrogenase Complex From Rhodobacter Capsulatus, PDB code: 8oie:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg302 b:60.1 occ:1.00 OG D:SER16 2.1 60.3 1.0 O2B D:ADP301 2.2 68.2 1.0 F1 D:AF3303 2.3 79.3 1.0 CB D:SER16 3.0 51.2 1.0 PB D:ADP301 3.3 55.6 1.0 O1B D:ADP301 3.4 69.0 1.0 OD2 D:ASP125 3.6 71.7 1.0 N D:SER16 3.8 52.4 1.0 AL D:AF3303 3.9 62.1 1.0 CA D:SER16 3.9 45.5 1.0 OD2 D:ASP40 4.0 72.8 1.0 OD1 D:ASP44 4.2 77.3 1.0 OG D:SER45 4.3 72.8 1.0 O3B D:ADP301 4.3 48.9 1.0 O3A D:ADP301 4.4 61.5 1.0 OD2 D:ASP44 4.4 73.9 1.0 CG D:ASP125 4.5 69.3 1.0 O1A D:ADP301 4.5 62.3 1.0 F3 D:AF3303 4.5 73.7 1.0 CG D:ASP44 4.6 73.9 1.0 O D:VAL126 4.6 65.5 1.0 OD1 D:ASP125 4.6 70.7 1.0 PA D:ADP301 4.7 61.4 1.0 O2A D:ADP301 4.8 66.5 1.0 CB D:LYS15 4.8 47.0 1.0 C D:LYS15 4.8 51.6 1.0

Magnesium binding site 2 out of 4 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg302 b:58.4 occ:1.00 OG E:SER16 2.1 66.1 1.0 O2B E:ADP301 2.2 69.6 1.0 F1 E:AF3303 2.3 74.6 1.0 CB E:SER16 3.2 51.7 1.0 PB E:ADP301 3.4 62.5 1.0 O3B E:ADP301 3.6 60.6 1.0 OD2 E:ASP125 3.6 77.1 1.0 AL E:AF3303 3.7 60.3 1.0 N E:SER16 3.9 56.9 1.0 OD2 E:ASP40 4.0 75.3 1.0 OG E:SER45 4.0 74.7 1.0 CA E:SER16 4.0 46.2 1.0 OD1 E:ASP44 4.3 83.1 1.0 O1B E:ADP301 4.3 61.4 1.0 CG E:ASP125 4.4 67.6 1.0 OD1 E:ASP125 4.5 67.2 1.0 O3A E:ADP301 4.5 61.8 1.0 F3 E:AF3303 4.6 72.3 1.0 OD2 E:ASP44 4.6 87.0 1.0 O E:VAL126 4.7 68.3 1.0 CG E:ASP44 4.8 83.2 1.0 CE E:LYS15 4.8 51.2 1.0 CB E:LYS15 4.8 48.2 1.0 O2A E:ADP301 4.9 66.2 1.0 CG E:ASP40 4.9 69.9 1.0 F2 E:AF3303 4.9 82.1 1.0 C E:LYS15 4.9 51.8 1.0 O1A E:ADP301 5.0 62.9 1.0 CB E:ASP40 5.0 61.9 1.0

Magnesium binding site 3 out of 4 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ I:Mg302 b:56.1 occ:1.00 OG I:SER16 2.1 59.5 1.0 O2B I:ADP301 2.2 67.7 1.0 F1 I:AF3303 2.5 76.6 1.0 CB I:SER16 3.0 51.2 1.0 PB I:ADP301 3.3 54.2 1.0 O1B I:ADP301 3.4 68.6 1.0 OD2 I:ASP125 3.6 72.2 1.0 N I:SER16 3.8 51.9 1.0 CA I:SER16 3.9 45.5 1.0 AL I:AF3303 3.9 61.5 1.0 OD2 I:ASP40 4.0 72.5 1.0 OD1 I:ASP44 4.2 76.2 1.0 OG I:SER45 4.3 71.9 1.0 O3A I:ADP301 4.3 61.0 1.0 O3B I:ADP301 4.3 48.2 1.0 OD2 I:ASP44 4.4 72.7 1.0 CG I:ASP125 4.4 68.9 1.0 OD1 I:ASP125 4.5 69.6 1.0 O1A I:ADP301 4.5 61.2 1.0 F3 I:AF3303 4.5 71.1 1.0 CG I:ASP44 4.6 73.2 1.0 PA I:ADP301 4.7 60.7 1.0 O2A I:ADP301 4.7 66.9 1.0 O I:VAL126 4.8 66.7 1.0 CB I:LYS15 4.8 47.4 1.0 C I:LYS15 4.8 51.9 1.0

Magnesium binding site 4 out of 4 in the Iron Nitrogenase Complex From Rhodobacter Capsulatus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ J:Mg302 b:61.2 occ:1.00 F1 J:AF3303 2.1 74.1 1.0 OG J:SER16 2.1 65.9 1.0 O2B J:ADP301 2.2 70.3 1.0 CB J:SER16 3.2 50.7 1.0 PB J:ADP301 3.4 63.2 1.0 O3B J:ADP301 3.5 60.9 1.0 AL J:AF3303 3.6 61.6 1.0 OD2 J:ASP125 3.7 78.5 1.0 N J:SER16 3.9 57.6 1.0 OD2 J:ASP40 3.9 77.9 1.0 OG J:SER45 4.0 76.5 1.0 CA J:SER16 4.0 46.7 1.0 O1B J:ADP301 4.3 61.9 1.0 OD1 J:ASP44 4.3 84.4 1.0 OD1 J:ASP125 4.3 65.2 1.0 CG J:ASP125 4.4 68.7 1.0 F3 J:AF3303 4.5 68.3 1.0 O3A J:ADP301 4.5 62.9 1.0 OD2 J:ASP44 4.6 87.9 1.0 O J:VAL126 4.7 69.7 1.0 F2 J:AF3303 4.7 80.0 1.0 CE J:LYS15 4.8 52.0 1.0 CB J:LYS15 4.8 48.2 1.0 CG J:ASP44 4.8 84.7 1.0 CG J:ASP40 4.9 71.3 1.0 O2A J:ADP301 4.9 67.1 1.0 C J:LYS15 5.0 52.5 1.0 O1A J:ADP301 5.0 64.7 1.0 CB J:ASP40 5.0 62.2 1.0

F.V.Schmidt, L.Schulz, J.Zarzycki, S.Prinz, N.N.Oehlmann, T.J.Erb, J.G.Rebelein. Structural Insights Into the Iron Nitrogenase Complex Nat.Struct.Mol.Biol. 2023.
ISSN: ESSN 1545-9985
DOI: 10.1038/S41594-023-01124-2