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Magnesium in PDB 1n2c: Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate

Enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate

All present enzymatic activity of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate:
1.18.6.1;

Protein crystallography data

The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1n2c was solved by H.Schindelin, C.Kisker, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 3.00
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 79.000, 299.700, 334.500, 90.00, 90.00, 90.00
R / Rfree (%) 20.8 / 23.8

Other elements in 1n2c:

The structure of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate also contains other interesting chemical elements:

Fluorine (F) 16 atoms
Molybdenum (Mo) 2 atoms
Aluminium (Al) 4 atoms
Iron (Fe) 38 atoms
Calcium (Ca) 2 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate (pdb code 1n2c). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1n2c:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in 1n2c

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Magnesium binding site 1 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
E:Mg292

b:24.0
occ:1.00
 F4 E:ALF293 2.2 24.0 1.0
OG E:SER16 2.4 17.4 1.0
F2 E:ALF293 2.8 24.0 1.0
OD2 E:ASP39 2.9 10.8 1.0
AL E:ALF293 3.3 24.0 1.0
O1B E:ADP291 3.6 24.0 1.0
CG E:ASP39 3.7 10.8 1.0
CB E:SER16 3.7 17.4 1.0
OD1 E:ASP43 3.7 13.4 1.0
CB E:ASP39 3.7 10.8 1.0
OD2 E:ASP43 3.7 13.4 1.0
OD2 E:ASP125 3.8 26.1 1.0
OD1 E:ASP125 3.9 26.1 1.0
CG E:ASP43 4.1 13.4 1.0
O E:VAL126 4.1 6.2 1.0
CG E:ASP125 4.1 26.1 1.0
O2B E:ADP291 4.3 24.0 1.0
OG E:SER44 4.4 27.6 1.0
CA E:LEU127 4.5 16.5 1.0
CG E:LYS15 4.5 22.1 1.0
PB E:ADP291 4.5 24.0 1.0
CA E:SER16 4.6 17.4 1.0
F1 E:ALF293 4.6 24.0 1.0
N E:SER16 4.7 17.4 1.0
NZ E:LYS41 4.7 16.8 1.0
C E:VAL126 4.7 6.2 1.0
OD1 E:ASP39 4.8 10.8 1.0
O E:ASP125 4.8 26.1 1.0
CD E:LYS15 4.9 22.1 1.0
N E:LEU127 4.9 16.5 1.0
F3 E:ALF293 4.9 24.0 1.0

Magnesium binding site 2 out of 4 in 1n2c

Go back to Magnesium Binding Sites List in 1n2c
Magnesium binding site 2 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
F:Mg292

b:24.0
occ:1.00
 F4 F:ALF293 2.2 24.0 1.0
OG F:SER16 2.4 21.4 1.0
F2 F:ALF293 2.9 24.0 1.0
OD2 F:ASP39 3.0 19.8 1.0
AL F:ALF293 3.4 24.0 1.0
O1B F:ADP291 3.6 24.0 1.0
CG F:ASP39 3.7 19.8 1.0
CB F:SER16 3.7 21.4 1.0
OD1 F:ASP43 3.7 17.4 1.0
CB F:ASP39 3.7 19.8 1.0
OD2 F:ASP43 3.7 17.4 1.0
OD2 F:ASP125 3.8 26.7 1.0
OD1 F:ASP125 3.9 26.7 1.0
CG F:ASP125 4.1 26.7 1.0
CG F:ASP43 4.1 17.4 1.0
O F:VAL126 4.1 26.4 1.0
O2B F:ADP291 4.3 24.0 1.0
OG F:SER44 4.4 21.5 1.0
CA F:LEU127 4.5 14.7 1.0
CG F:LYS15 4.5 32.0 1.0
PB F:ADP291 4.5 24.0 1.0
CA F:SER16 4.6 21.4 1.0
F1 F:ALF293 4.6 24.0 1.0
N F:SER16 4.6 21.4 1.0
C F:VAL126 4.7 26.4 1.0
NZ F:LYS41 4.7 29.7 1.0
OD1 F:ASP39 4.8 19.8 1.0
O F:ASP125 4.8 26.7 1.0
CD F:LYS15 4.9 32.0 1.0
N F:LEU127 4.9 14.7 1.0
F3 F:ALF293 4.9 24.0 1.0

Magnesium binding site 3 out of 4 in 1n2c

Go back to Magnesium Binding Sites List in 1n2c
Magnesium binding site 3 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
G:Mg292

b:24.0
occ:1.00
 F4 G:ALF293 2.2 24.0 1.0
OG G:SER16 2.4 7.2 1.0
F2 G:ALF293 2.8 24.0 1.0
OD2 G:ASP39 2.9 13.3 1.0
AL G:ALF293 3.4 24.0 1.0
O1B G:ADP291 3.5 24.0 1.0
CG G:ASP39 3.7 13.3 1.0
CB G:SER16 3.7 7.2 1.0
CB G:ASP39 3.7 13.3 1.0
OD1 G:ASP43 3.7 25.0 1.0
OD2 G:ASP43 3.7 25.0 1.0
OD2 G:ASP125 3.8 25.7 1.0
OD1 G:ASP125 3.9 25.7 1.0
CG G:ASP43 4.1 25.0 1.0
CG G:ASP125 4.1 25.7 1.0
O G:VAL126 4.1 9.9 1.0
O2B G:ADP291 4.3 24.0 1.0
OG G:SER44 4.4 29.4 1.0
CA G:LEU127 4.5 12.2 1.0
CG G:LYS15 4.5 32.1 1.0
PB G:ADP291 4.5 24.0 1.0
CA G:SER16 4.6 7.2 1.0
F1 G:ALF293 4.6 24.0 1.0
N G:SER16 4.7 7.2 1.0
C G:VAL126 4.7 9.9 1.0
NZ G:LYS41 4.7 32.0 1.0
OD1 G:ASP39 4.8 13.3 1.0
O G:ASP125 4.8 25.7 1.0
CD G:LYS15 4.8 32.1 1.0
N G:LEU127 4.9 12.2 1.0
F3 G:ALF293 4.9 24.0 1.0

Magnesium binding site 4 out of 4 in 1n2c

Go back to Magnesium Binding Sites List in 1n2c
Magnesium binding site 4 out of 4 in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate within 5.0Å range:
probe atom residue distance (Å) B Occ
H:Mg292

b:24.0
occ:1.00
 F4 H:ALF293 2.1 24.0 1.0
OG H:SER16 2.3 22.9 1.0
F2 H:ALF293 2.8 24.0 1.0
OD2 H:ASP39 3.0 15.3 1.0
AL H:ALF293 3.3 24.0 1.0
O1B H:ADP291 3.6 24.0 1.0
CG H:ASP39 3.7 15.3 1.0
CB H:SER16 3.7 22.9 1.0
OD2 H:ASP43 3.7 28.4 1.0
OD1 H:ASP43 3.7 28.4 1.0
CB H:ASP39 3.7 15.3 1.0
OD2 H:ASP125 3.8 21.8 1.0
OD1 H:ASP125 3.9 21.8 1.0
CG H:ASP43 4.1 28.4 1.0
CG H:ASP125 4.1 21.8 1.0
O H:VAL126 4.1 20.2 1.0
O2B H:ADP291 4.3 24.0 1.0
OG H:SER44 4.4 20.7 1.0
CA H:LEU127 4.5 28.5 1.0
CG H:LYS15 4.5 27.1 1.0
PB H:ADP291 4.5 24.0 1.0
CA H:SER16 4.6 22.9 1.0
F1 H:ALF293 4.6 24.0 1.0
N H:SER16 4.6 22.9 1.0
NZ H:LYS41 4.7 23.2 1.0
C H:VAL126 4.7 20.2 1.0
OD1 H:ASP39 4.8 15.3 1.0
O H:ASP125 4.8 21.8 1.0
CD H:LYS15 4.9 27.1 1.0
N H:LEU127 4.9 28.5 1.0
F3 H:ALF293 4.9 24.0 1.0

Reference:

H.Schindelin, C.Kisker, J.L.Schlessman, J.B.Howard, D.C.Rees. Structure of Adp X AIF4(-)-Stabilized Nitrogenase Complex and Its Implications For Signal Transduction. Nature V. 387 370 1997.
ISSN: ISSN 0028-0836
PubMed: 9163420
DOI: 10.1038/387370A0
Page generated: Tue Aug 13 09:21:04 2024

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