Magnesium in PDB 9cu2: Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (C2 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (C2 Symmetry):
1.18.6.1;

The structure of Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (C2 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 (C2 Symmetry) (pdb code 9cu2). 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 (C2 Symmetry), PDB code: 9cu2:
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 (C2 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 (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg302 b:38.8 occ:1.00 O3B E:ADP301 2.3 35.8 1.0 OG E:SER17 2.6 34.4 1.0 O1A E:ADP301 3.2 40.9 1.0 CB E:SER17 3.3 28.1 1.0 NZ E:LYS42 3.4 42.6 1.0 PB E:ADP301 3.5 33.5 1.0 CE E:LYS42 3.6 42.4 1.0 O3A E:ADP301 3.6 41.3 1.0 PA E:ADP301 3.7 36.7 1.0 O2B E:ADP301 4.0 38.6 1.0 O2A E:ADP301 4.0 36.8 1.0 CB E:ASP44 4.4 43.8 1.0 CA E:SER17 4.6 31.1 1.0 O E:ASP44 4.6 41.9 1.0 O1B E:ADP301 4.7 36.2 1.0 CD E:LYS42 4.7 34.0 1.0 CG E:LYS42 4.7 30.5 1.0 OD2 E:ASP40 4.7 40.6 1.0 C E:ASP44 4.8 37.4 1.0 N E:SER17 4.8 28.9 1.0 O E:HOH419 4.8 47.9 1.0 OD2 E:ASP126 4.9 36.9 1.0

Magnesium binding site 2 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (C2 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 (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ F:Mg303 b:33.5 occ:1.00 O2B F:ADP302 2.1 30.9 1.0 OG F:SER17 2.8 30.5 1.0 O F:HOH413 3.2 30.9 1.0 PB F:ADP302 3.2 24.2 1.0 OD2 F:ASP40 3.4 31.7 1.0 O3B F:ADP302 3.4 28.3 1.0 OD1 F:ASP44 3.6 41.3 1.0 CB F:SER17 3.8 29.9 1.0 O1B F:ADP302 4.2 30.0 1.0 CG F:ASP44 4.3 41.0 1.0 OD2 F:ASP126 4.3 28.8 1.0 O2A F:ADP302 4.3 41.9 1.0 O3A F:ADP302 4.4 38.7 1.0 CG F:ASP40 4.4 26.0 1.0 OD2 F:ASP44 4.4 47.0 1.0 N F:SER17 4.5 31.0 1.0 PA F:ADP302 4.7 39.0 1.0 CA F:SER17 4.7 32.3 1.0 O1A F:ADP302 4.7 34.4 1.0 CB F:ASP40 4.8 25.5 1.0 CE F:LYS16 4.9 21.0 1.0 CB F:LYS42 5.0 28.9 1.0

Magnesium binding site 3 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (C2 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 (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ L:Mg302 b:37.7 occ:1.00 O3A L:ADP301 2.4 55.8 1.0 O2B L:ADP301 2.5 42.1 1.0 OG L:SER17 2.5 35.6 1.0 OD1 L:ASP44 2.7 47.5 1.0 PB L:ADP301 3.0 42.4 1.0 CB L:SER17 3.4 36.0 1.0 CG L:ASP44 3.6 49.8 1.0 O1B L:ADP301 3.6 46.4 1.0 PA L:ADP301 3.7 47.1 1.0 OD2 L:ASP44 3.7 55.8 1.0 NZ L:LYS42 3.8 33.2 1.0 O1A L:ADP301 3.8 45.8 1.0 CE L:LYS42 4.0 27.1 1.0 O3B L:ADP301 4.3 42.8 1.0 OD2 L:ASP40 4.4 32.3 1.0 O2A L:ADP301 4.6 42.7 1.0 CA L:SER17 4.6 33.8 1.0 N L:SER17 4.6 33.4 1.0 O5' L:ADP301 4.8 46.6 1.0 C L:ASP44 4.9 32.9 1.0 OD2 L:ASP126 5.0 37.8 1.0 O L:ASP44 5.0 37.9 1.0 CB L:ASP44 5.0 42.1 1.0

Magnesium binding site 4 out of 4 in the Azotobacter Vinelandii Filamentous 2:2:1 Mofep:Fep:Fesii-Complex (C2 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 (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ M:Mg303 b:34.5 occ:1.00 O2B M:ADP302 2.1 33.3 1.0 OG M:SER17 2.5 36.2 1.0 O M:HOH407 3.2 32.8 1.0 PB M:ADP302 3.2 30.4 1.0 OD1 M:ASP44 3.4 39.2 1.0 O3B M:ADP302 3.5 33.4 1.0 CB M:SER17 3.7 32.9 1.0 OD2 M:ASP40 3.9 40.8 1.0 OD2 M:ASP44 4.0 43.1 1.0 CG M:ASP40 4.1 33.7 1.0 CG M:ASP44 4.1 38.8 1.0 O1B M:ADP302 4.1 28.6 1.0 OD2 M:ASP126 4.2 34.0 1.0 O2A M:ADP302 4.3 50.1 1.0 O3A M:ADP302 4.4 43.0 1.0 CD M:LYS42 4.4 36.0 1.0 OD1 M:ASP40 4.4 35.3 1.0 N M:SER17 4.5 30.7 1.0 CB M:ASP40 4.5 31.5 1.0 CG M:LYS42 4.6 31.8 1.0 CA M:SER17 4.7 28.8 1.0 PA M:ADP302 4.7 41.3 1.0 O1A M:ADP302 4.8 32.4 1.0 NZ M:LYS16 4.9 27.9 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