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Aluminium 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
Magnesium (Mg) 4 atoms
Iron (Fe) 38 atoms
Calcium (Ca) 2 atoms

Aluminium Binding Sites:

The binding sites of Aluminium 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 Aluminium atom.
In total 4 binding sites of Aluminium where determined in the Nitrogenase Complex From Azotobacter Vinelandii Stabilized By Adp- Tetrafluoroaluminate, PDB code: 1n2c:
Jump to Aluminium binding site number: 1; 2; 3; 4;

Aluminium binding site 1 out of 4 in 1n2c

Go back to Aluminium Binding Sites List in 1n2c
Aluminium 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 Aluminium with other atoms in the Al 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:Al293

b:24.0
occ:1.00
 AL E:ALF293 0.0 24.0 1.0
F2 E:ALF293 1.8 24.0 1.0
F3 E:ALF293 1.8 24.0 1.0
F1 E:ALF293 1.8 24.0 1.0
F4 E:ALF293 1.8 24.0 1.0
O1B E:ADP291 1.9 24.0 1.0
PB E:ADP291 2.9 24.0 1.0
O3B E:ADP291 3.1 24.0 1.0
MG E:MG292 3.3 24.0 1.0
NZ F:LYS10 3.5 13.4 1.0
O2B E:ADP291 3.7 24.0 1.0
OD2 E:ASP39 3.7 10.8 1.0
N E:GLY128 3.9 19.5 1.0
N E:GLY12 3.9 2.0 1.0
NZ E:LYS15 4.1 22.1 1.0
O3A E:ADP291 4.2 24.0 1.0
OG E:SER16 4.2 17.4 1.0
CA E:GLY12 4.5 2.0 1.0
CE F:LYS10 4.5 13.4 1.0
CG E:LYS15 4.6 22.1 1.0
CA E:GLY128 4.6 19.5 1.0
CA E:LEU127 4.6 16.5 1.0
CD E:LYS15 4.6 22.1 1.0
C E:LEU127 4.7 16.5 1.0
OD1 F:ASP129 4.8 37.7 1.0
OD2 F:ASP129 4.9 37.7 1.0
NZ E:LYS41 4.9 16.8 1.0
CG E:ASP39 4.9 10.8 1.0
C E:GLY11 4.9 29.9 1.0
O2A E:ADP291 4.9 24.0 1.0
CE E:LYS15 5.0 22.1 1.0
CA E:GLY11 5.0 29.9 1.0

Aluminium binding site 2 out of 4 in 1n2c

Go back to Aluminium Binding Sites List in 1n2c
Aluminium 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 Aluminium with other atoms in the Al 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:Al293

b:24.0
occ:1.00
 AL F:ALF293 0.0 24.0 1.0
F3 F:ALF293 1.8 24.0 1.0
F2 F:ALF293 1.8 24.0 1.0
F1 F:ALF293 1.8 24.0 1.0
F4 F:ALF293 1.8 24.0 1.0
O1B F:ADP291 1.9 24.0 1.0
PB F:ADP291 2.9 24.0 1.0
O3B F:ADP291 3.1 24.0 1.0
MG F:MG292 3.4 24.0 1.0
NZ E:LYS10 3.4 21.1 1.0
O2B F:ADP291 3.7 24.0 1.0
OD2 F:ASP39 3.7 19.8 1.0
N F:GLY128 3.9 44.3 1.0
N F:GLY12 3.9 24.7 1.0
NZ F:LYS15 4.1 32.0 1.0
O3A F:ADP291 4.2 24.0 1.0
OG F:SER16 4.2 21.4 1.0
CE E:LYS10 4.4 21.1 1.0
CA F:GLY12 4.5 24.7 1.0
CG F:LYS15 4.6 32.0 1.0
CA F:GLY128 4.6 44.3 1.0
CA F:LEU127 4.6 14.7 1.0
CD F:LYS15 4.6 32.0 1.0
C F:LEU127 4.7 14.7 1.0
OD1 E:ASP129 4.9 22.6 1.0
CG F:ASP39 4.9 19.8 1.0
NZ F:LYS41 4.9 29.7 1.0
OD2 E:ASP129 4.9 22.6 1.0
C F:GLY11 4.9 5.3 1.0
O2A F:ADP291 4.9 24.0 1.0
CE F:LYS15 5.0 32.0 1.0
CA F:GLY11 5.0 5.3 1.0

Aluminium binding site 3 out of 4 in 1n2c

Go back to Aluminium Binding Sites List in 1n2c
Aluminium 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 Aluminium with other atoms in the Al 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:Al293

b:24.0
occ:1.00
 AL G:ALF293 0.0 24.0 1.0
F3 G:ALF293 1.8 24.0 1.0
F2 G:ALF293 1.8 24.0 1.0
F1 G:ALF293 1.8 24.0 1.0
O1B G:ADP291 1.8 24.0 1.0
F4 G:ALF293 1.8 24.0 1.0
PB G:ADP291 2.9 24.0 1.0
O3B G:ADP291 3.1 24.0 1.0
MG G:MG292 3.4 24.0 1.0
NZ H:LYS10 3.5 10.4 1.0
O2B G:ADP291 3.7 24.0 1.0
OD2 G:ASP39 3.7 13.3 1.0
N G:GLY12 3.9 22.7 1.0
N G:GLY128 3.9 16.3 1.0
NZ G:LYS15 4.1 32.1 1.0
O3A G:ADP291 4.1 24.0 1.0
OG G:SER16 4.2 7.2 1.0
CA G:GLY12 4.4 22.7 1.0
CE H:LYS10 4.5 10.4 1.0
CG G:LYS15 4.6 32.1 1.0
CA G:GLY128 4.6 16.3 1.0
CD G:LYS15 4.6 32.1 1.0
CA G:LEU127 4.6 12.2 1.0
C G:LEU127 4.7 12.2 1.0
OD1 H:ASP129 4.7 31.6 1.0
OD2 H:ASP129 4.8 31.6 1.0
C G:GLY11 4.9 38.0 1.0
NZ G:LYS41 4.9 32.0 1.0
CG G:ASP39 4.9 13.3 1.0
O2A G:ADP291 4.9 24.0 1.0
CE G:LYS15 5.0 32.1 1.0
CA G:GLY11 5.0 38.0 1.0

Aluminium binding site 4 out of 4 in 1n2c

Go back to Aluminium Binding Sites List in 1n2c
Aluminium 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 Aluminium with other atoms in the Al 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:Al293

b:24.0
occ:1.00
 AL H:ALF293 0.0 24.0 1.0
F2 H:ALF293 1.8 24.0 1.0
F3 H:ALF293 1.8 24.0 1.0
F1 H:ALF293 1.8 24.0 1.0
F4 H:ALF293 1.8 24.0 1.0
O1B H:ADP291 1.9 24.0 1.0
PB H:ADP291 3.0 24.0 1.0
O3B H:ADP291 3.1 24.0 1.0
MG H:MG292 3.3 24.0 1.0
NZ G:LYS10 3.4 25.2 1.0
O2B H:ADP291 3.7 24.0 1.0
OD2 H:ASP39 3.7 15.3 1.0
N H:GLY128 3.9 34.0 1.0
N H:GLY12 3.9 28.5 1.0
NZ H:LYS15 4.1 27.1 1.0
O3A H:ADP291 4.2 24.0 1.0
OG H:SER16 4.2 22.9 1.0
CE G:LYS10 4.3 25.2 1.0
CA H:GLY12 4.5 28.5 1.0
CG H:LYS15 4.6 27.1 1.0
CA H:GLY128 4.6 34.0 1.0
CA H:LEU127 4.6 28.5 1.0
CD H:LYS15 4.6 27.1 1.0
C H:LEU127 4.7 28.5 1.0
CG H:ASP39 4.9 15.3 1.0
NZ H:LYS41 4.9 23.2 1.0
C H:GLY11 4.9 21.9 1.0
O2A H:ADP291 4.9 24.0 1.0
OD1 G:ASP129 5.0 31.2 1.0
CE H:LYS15 5.0 27.1 1.0
CA H:GLY11 5.0 21.9 1.0
OD2 G:ASP129 5.0 31.2 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: Sun Jul 6 21:36:23 2025

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