Atomistry » Magnesium » PDB 1mum-1n6i » 1n2c
Atomistry »
  Magnesium »
    PDB 1mum-1n6i »
      1n2c »

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

Go back to Magnesium Binding Sites List in 1n2c
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

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy