Atomistry » Aluminium » PDB 1a6e-1tx4 » 1n2c
Atomistry »
  Aluminium »
    PDB 1a6e-1tx4 »
      1n2c »

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: Sat Dec 12 01:30:23 2020

Last articles

Zn in 7O75
Zn in 7O73
Zn in 7O4I
Zn in 7O72
Zn in 7O4J
Zn in 7NVR
Zn in 7NVY
Zn in 7NVZ
Zn in 7NW0
Zn in 7O4K
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy