Magnesium in PDB 9cu1: Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry):
1.18.6.1;

The structure of Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry) also contains other interesting chemical elements:

Molybdenum	(Mo)	4 atoms
Iron	(Fe)	76 atoms

The binding sites of Magnesium atom in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry) (pdb code 9cu1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry), PDB code: 9cu1:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; 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 Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg302 b:131.7 occ:1.00 O3B E:ADP301 2.1 152.3 1.0 OG E:SER17 2.1 144.6 1.0 CB E:SER17 3.2 144.1 1.0 PB E:ADP301 3.3 162.9 1.0 O1A E:ADP301 3.4 153.1 1.0 O3A E:ADP301 3.6 160.7 1.0 PA E:ADP301 3.8 162.0 1.0 O2A E:ADP301 3.9 152.5 1.0 O2B E:ADP301 4.0 156.9 1.0 CE E:LYS42 4.1 136.6 1.0 NZ E:LYS42 4.2 134.6 1.0 N E:SER17 4.3 142.1 1.0 CA E:SER17 4.3 141.4 1.0 OD1 E:ASP40 4.5 129.4 1.0 O1B E:ADP301 4.5 151.4 1.0 OD2 E:ASP126 4.6 133.4 1.0 CB E:ASP44 4.8 142.1 1.0 OD1 E:ASP44 4.9 139.2 1.0 CG E:ASP40 4.9 122.5 1.0

Magnesium binding site 2 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; 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 Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg303 b:136.4 occ:1.00 O2B F:ADP302 2.0 139.1 1.0 OG F:SER17 2.0 140.3 1.0 PB F:ADP302 3.2 139.8 1.0 CB F:SER17 3.3 134.4 1.0 OD2 F:ASP40 3.4 132.7 1.0 O3B F:ADP302 3.6 134.9 1.0 OD1 F:ASP44 3.8 140.2 1.0 N F:SER17 3.9 129.1 1.0 OD2 F:ASP126 3.9 131.5 1.0 O1B F:ADP302 4.1 135.5 1.0 CA F:SER17 4.1 129.5 1.0 O3A F:ADP302 4.4 145.2 1.0 CG F:ASP40 4.4 127.1 1.0 O2A F:ADP302 4.5 144.5 1.0 CG F:ASP44 4.6 141.5 1.0 O1A F:ADP302 4.6 135.8 1.0 CE F:LYS16 4.6 114.1 1.0 PA F:ADP302 4.7 149.4 1.0 CG F:ASP126 4.7 127.1 1.0 OD2 F:ASP44 4.7 145.7 1.0 CB F:ASP40 4.7 124.9 1.0 OD1 F:ASP126 4.7 128.1 1.0 CB F:LYS16 4.8 132.9 1.0 C F:LYS16 4.9 128.5 1.0 CE E:MET157 5.0 140.5 1.0

Magnesium binding site 3 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg302 b:139.8 occ:1.00 OG L:SER17 2.0 132.0 1.0 O3A L:ADP301 2.0 147.4 1.0 O2B L:ADP301 2.4 129.6 1.0 CB L:SER17 2.8 132.8 1.0 PB L:ADP301 2.8 140.5 1.0 OD2 L:ASP44 3.1 137.8 1.0 OD1 L:ASP44 3.2 136.1 1.0 PA L:ADP301 3.3 149.6 1.0 O1A L:ADP301 3.5 144.1 1.0 CG L:ASP44 3.5 137.2 1.0 O1B L:ADP301 3.8 139.7 1.0 O3B L:ADP301 3.9 139.0 1.0 N L:SER17 3.9 128.1 1.0 CA L:SER17 3.9 128.4 1.0 O2A L:ADP301 4.0 137.7 1.0 NZ L:LYS42 4.2 132.3 1.0 OD2 L:ASP40 4.3 122.3 1.0 O5' L:ADP301 4.5 146.8 1.0 OD2 L:ASP126 4.8 120.4 1.0 O L:HOH404 4.8 135.0 1.0 O L:ASP44 5.0 131.7 1.0

Magnesium binding site 4 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (Termini; C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ M:Mg302 b:118.2 occ:1.00 OG M:SER17 2.0 128.0 1.0 O2B M:ADP301 2.1 132.4 1.0 PB M:ADP301 3.3 139.7 1.0 CB M:SER17 3.3 125.6 1.0 OD1 M:ASP44 3.4 131.1 1.0 O3B M:ADP301 3.8 131.8 1.0 OD2 M:ASP126 3.8 116.4 1.0 O1B M:ADP301 4.0 131.1 1.0 CG M:ASP44 4.1 128.6 1.0 CD M:LYS42 4.1 131.6 1.0 OD2 M:ASP44 4.1 130.3 1.0 OD2 M:ASP40 4.2 114.2 1.0 CG M:ASP40 4.2 112.7 1.0 N M:SER17 4.3 125.9 1.0 CA M:SER17 4.3 124.6 1.0 CB M:ASP40 4.4 109.8 1.0 O2A M:ADP301 4.5 147.0 1.0 O3A M:ADP301 4.5 143.6 1.0 OD1 M:ASP40 4.6 113.9 1.0 CG M:LYS42 4.6 120.7 1.0 OD1 M:ASP126 4.6 117.0 1.0 CG M:ASP126 4.7 117.0 1.0 PA M:ADP301 4.8 150.3 1.0 O1A M:ADP301 4.9 135.2 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