Aluminium 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:

Iron	(Fe)	40 atoms
Fluorine	(F)	12 atoms
Magnesium	(Mg)	4 atoms

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

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


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 1 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ D:Al303 b:62.1 occ:1.00 AL D:AF3303 0.0 62.1 1.0 F2 D:AF3303 1.8 73.4 1.0 F3 D:AF3303 1.8 73.7 1.0 F1 D:AF3303 1.8 79.3 1.0 O1B D:ADP301 1.9 69.0 1.0 PB D:ADP301 3.2 55.6 1.0 O3B D:ADP301 3.8 48.9 1.0 O2B D:ADP301 3.8 68.2 1.0 MG D:MG302 3.9 60.1 1.0 N D:GLY12 3.9 48.2 1.0 NZ D:LYS42 3.9 62.6 1.0 NZ D:LYS15 4.0 49.6 1.0 OD2 D:ASP40 4.0 72.8 1.0 N D:GLY128 4.0 55.4 1.0 CE D:LYS15 4.3 44.6 1.0 NZ E:LYS10 4.4 56.4 1.0 OD2 E:ASP129 4.4 74.4 1.0 O3A D:ADP301 4.4 61.5 1.0 OD1 E:ASP129 4.5 70.3 1.0 CA D:LEU127 4.6 46.6 1.0 C D:LEU127 4.6 55.9 1.0 CA D:GLY12 4.6 51.4 1.0 CA D:GLY11 4.7 50.3 1.0 CA D:GLY128 4.7 49.0 1.0 C D:GLY11 4.8 49.3 1.0 CG E:ASP129 4.9 73.3 1.0 CE E:LYS10 4.9 57.5 1.0

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


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 2 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ E:Al303 b:60.3 occ:1.00 AL E:AF3303 0.0 60.3 1.0 F3 E:AF3303 1.8 72.3 1.0 F2 E:AF3303 1.8 82.1 1.0 F1 E:AF3303 1.8 74.6 1.0 O3B E:ADP301 1.8 60.6 1.0 PB E:ADP301 3.2 62.5 1.0 O2B E:ADP301 3.7 69.6 1.0 MG E:MG302 3.7 58.4 1.0 O1B E:ADP301 3.8 61.4 1.0 N E:GLY12 3.8 56.5 1.0 NZ E:LYS42 4.0 67.9 1.0 NZ E:LYS15 4.1 45.0 1.0 NZ D:LYS10 4.2 43.4 1.0 OD2 E:ASP40 4.2 75.3 1.0 N E:GLY128 4.2 50.6 1.0 O3A E:ADP301 4.4 61.8 1.0 CE E:LYS15 4.4 51.2 1.0 CA E:GLY11 4.5 54.6 1.0 OD1 D:ASP129 4.5 61.2 1.0 CA E:GLY12 4.6 47.5 1.0 CA E:LEU127 4.6 54.5 1.0 C E:GLY11 4.7 58.5 1.0 CE D:LYS10 4.7 41.9 1.0 C E:LEU127 4.8 55.3 1.0 OD2 D:ASP129 4.8 70.0 1.0 CA E:GLY128 5.0 52.5 1.0 CB E:LEU127 5.0 52.0 1.0

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


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 3 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ I:Al303 b:61.5 occ:1.00 AL I:AF3303 0.0 61.5 1.0 F1 I:AF3303 1.8 76.6 1.0 F2 I:AF3303 1.8 70.9 1.0 F3 I:AF3303 1.8 71.1 1.0 O1B I:ADP301 1.8 68.6 1.0 PB I:ADP301 3.2 54.2 1.0 O2B I:ADP301 3.9 67.7 1.0 O3B I:ADP301 3.9 48.2 1.0 MG I:MG302 3.9 56.1 1.0 NZ I:LYS42 3.9 62.9 1.0 N I:GLY12 3.9 49.3 1.0 N I:GLY128 4.0 54.5 1.0 OD2 I:ASP40 4.0 72.5 1.0 NZ I:LYS15 4.0 49.5 1.0 OD2 J:ASP129 4.3 77.7 1.0 CE I:LYS15 4.3 44.7 1.0 OD1 J:ASP129 4.4 73.2 1.0 NZ J:LYS10 4.4 56.4 1.0 O3A I:ADP301 4.4 61.0 1.0 CA I:LEU127 4.6 46.7 1.0 C I:LEU127 4.6 55.6 1.0 CA I:GLY12 4.7 50.7 1.0 CA I:GLY11 4.7 50.5 1.0 CA I:GLY128 4.7 49.2 1.0 CG J:ASP129 4.8 75.9 1.0 C I:GLY11 4.8 50.0 1.0 CE J:LYS10 4.9 58.8 1.0

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


Mono view


Stereo pair view

A full contact list of Aluminium with other atoms in the Al binding site number 4 of Iron Nitrogenase Complex From Rhodobacter Capsulatus within 5.0Å range: probe atom residue distance (Å) B Occ J:Al303 b:61.6 occ:1.00 AL J:AF3303 0.0 61.6 1.0 F3 J:AF3303 1.8 68.3 1.0 F2 J:AF3303 1.8 80.0 1.0 F1 J:AF3303 1.8 74.1 1.0 O3B J:ADP301 1.9 60.9 1.0 PB J:ADP301 3.1 63.2 1.0 MG J:MG302 3.6 61.2 1.0 O2B J:ADP301 3.6 70.3 1.0 O1B J:ADP301 3.8 61.9 1.0 N J:GLY12 3.9 56.0 1.0 NZ J:LYS15 4.0 45.2 1.0 NZ J:LYS42 4.1 69.4 1.0 OD2 J:ASP40 4.1 77.9 1.0 N J:GLY128 4.2 52.2 1.0 CE J:LYS15 4.3 52.0 1.0 NZ I:LYS10 4.3 43.4 1.0 O3A J:ADP301 4.4 62.9 1.0 CA J:LEU127 4.4 53.8 1.0 OD1 I:ASP129 4.5 60.3 1.0 CA J:GLY11 4.5 53.6 1.0 C J:LEU127 4.7 53.9 1.0 CA J:GLY12 4.7 47.5 1.0 C J:GLY11 4.8 57.0 1.0 OD2 I:ASP129 4.8 68.4 1.0 CB J:LEU127 4.8 51.5 1.0 CE I:LYS10 4.9 42.1 1.0 CA J:GLY128 4.9 55.5 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