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Magnesium in PDB 7uta: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

Enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction:
1.18.6.1;

Other elements in 7uta:

The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms
Iron (Fe) 40 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction (pdb code 7uta). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction, PDB code: 7uta:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 7uta

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Magnesium binding site 1 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg302

b:56.8
occ:1.00
 O1B E:ADP303 2.4 73.8 1.0
OG E:SER16 2.9 38.5 1.0
BE E:0BE304 3.0 30.0 1.0
OD1 E:ASP43 3.2 53.5 1.0
OD2 E:ASP39 3.3 47.9 1.0
PB E:ADP303 3.5 73.8 1.0
O2B E:ADP303 3.6 73.8 1.0
CB E:SER16 3.8 40.5 1.0
O2A E:ADP303 3.9 73.8 1.0
CG E:ASP43 4.1 50.1 1.0
CG E:ASP39 4.2 49.2 1.0
OD2 E:ASP43 4.2 50.3 1.0
OD2 E:ASP125 4.2 44.9 1.0
OG E:SER44 4.5 47.4 1.0
O3A E:ADP303 4.5 73.8 1.0
O3B E:ADP303 4.6 73.8 1.0
CB E:ASP39 4.7 48.0 1.0
N E:SER16 4.8 33.1 1.0
NZ E:LYS41 4.8 46.7 1.0
PA E:ADP303 4.9 73.8 1.0
CA E:SER16 4.9 35.9 1.0
CE E:LYS41 5.0 46.0 1.0

Magnesium binding site 2 out of 4 in 7uta

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Magnesium binding site 2 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg301

b:65.1
occ:1.00
 O2B F:ADP302 2.4 81.9 1.0
BE F:0BE303 3.1 30.0 1.0
PB F:ADP302 3.4 81.9 1.0
O3B F:ADP302 3.5 81.9 1.0
OG F:SER16 3.7 48.4 1.0
CB F:SER16 4.0 45.5 1.0
O2A F:ADP302 4.0 81.9 1.0
CE F:LYS15 4.0 44.9 1.0
N F:SER16 4.2 39.1 1.0
CB F:LYS15 4.3 43.4 1.0
OD1 F:ASP125 4.3 47.5 1.0
O1B F:ADP302 4.4 81.9 1.0
O3A F:ADP302 4.6 81.9 1.0
NZ F:LYS41 4.7 55.8 1.0
PA F:ADP302 4.7 81.9 1.0
CA F:SER16 4.7 41.3 1.0
O F:VAL126 4.8 46.8 1.0
O1A F:ADP302 4.8 81.9 1.0
OD1 F:ASP43 4.9 61.8 1.0
NZ F:LYS15 4.9 42.0 1.0

Magnesium binding site 3 out of 4 in 7uta

Go back to Magnesium Binding Sites List in 7uta
Magnesium binding site 3 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg302

b:62.0
occ:1.00
 OG G:SER16 2.0 41.1 1.0
O2B G:ADP303 2.3 73.8 1.0
CB G:SER16 3.1 42.0 1.0
OD1 G:ASP43 3.3 55.3 1.0
OD2 G:ASP125 3.4 45.0 1.0
BE G:0BE304 3.5 30.0 1.0
PB G:ADP303 3.8 73.8 1.0
OD2 G:ASP39 4.0 50.3 1.0
CG G:ASP43 4.0 53.9 1.0
OD2 G:ASP43 4.0 53.6 1.0
N G:SER16 4.1 29.5 1.0
CA G:SER16 4.1 33.8 1.0
CG G:ASP125 4.3 46.6 1.0
OG G:SER44 4.4 45.7 1.0
O3B G:ADP303 4.4 73.8 1.0
OD1 G:ASP125 4.5 45.0 1.0
O1B G:ADP303 4.6 73.8 1.0
O1A G:ADP303 4.6 73.8 1.0
O3A G:ADP303 4.7 73.8 1.0
NZ G:LYS15 4.8 45.7 1.0
O2A G:ADP303 4.8 73.8 1.0
CG G:ASP39 4.8 53.7 1.0
CB G:ASP39 4.9 51.0 1.0
PA G:ADP303 4.9 73.8 1.0
CE H:MET156 5.0 52.4 1.0

Magnesium binding site 4 out of 4 in 7uta

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Magnesium binding site 4 out of 4 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg301

b:72.8
occ:1.00
 O1B H:ADP302 2.6 93.5 1.0
OG H:SER16 2.7 33.5 1.0
BE H:0BE303 3.5 30.0 1.0
O2B H:ADP302 3.5 93.5 1.0
O1A H:ADP302 3.6 93.5 1.0
PB H:ADP302 3.6 93.5 1.0
CB H:SER16 3.9 37.4 1.0
OG H:SER44 4.1 47.6 1.0
N H:SER16 4.5 32.9 1.0
OD1 H:ASP43 4.6 50.8 1.0
PA H:ADP302 4.6 93.5 1.0
OD1 H:ASP125 4.6 48.9 1.0
O3A H:ADP302 4.6 93.5 1.0
NZ G:LYS10 4.7 42.0 1.0
O3B H:ADP302 4.7 93.5 1.0
CA H:SER16 4.9 34.2 1.0

Reference:

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641
Page generated: Thu Oct 3 10:12:32 2024

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