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Calcium 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
Aluminium (Al) 4 atoms
Iron (Fe) 38 atoms

Calcium Binding Sites:

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

Calcium binding site 1 out of 2 in 1n2c

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


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca 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
B:Ca524

b:24.0
occ:1.00
O D:ARG108 2.2 23.6 1.0
OD2 B:ASP357 2.4 17.6 1.0
OE2 D:GLU109 2.4 15.4 1.0
OD2 B:ASP353 2.5 28.2 1.0
OD1 B:ASP353 2.8 28.2 1.0
NZ C:LYS433 2.9 27.9 1.0
CG B:ASP353 3.0 28.2 1.0
OD1 B:ASP357 3.0 17.6 1.0
CG B:ASP357 3.0 17.6 1.0
CD D:GLU109 3.2 15.4 1.0
C D:ARG108 3.4 23.6 1.0
OE1 D:GLU109 3.7 15.4 1.0
CA D:GLU109 4.0 15.4 1.0
N D:GLU109 4.1 15.4 1.0
CG D:GLU109 4.1 15.4 1.0
CD1 C:PHE429 4.2 27.9 1.0
CE C:LYS433 4.3 27.9 1.0
O B:ASP353 4.3 28.2 1.0
CB B:ASP353 4.4 28.2 1.0
CB B:ASP357 4.5 17.6 1.0
CB C:PHE429 4.5 27.9 1.0
CB D:GLU109 4.6 15.4 1.0
CG C:PHE429 4.6 27.9 1.0
CB D:ARG108 4.6 23.6 1.0
CA D:ARG108 4.6 23.6 1.0
C B:ASP353 4.8 28.2 1.0
CD C:LYS433 4.9 27.9 1.0
O D:PHE107 4.9 11.5 1.0
CE1 C:PHE429 5.0 27.9 1.0

Calcium binding site 2 out of 2 in 1n2c

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


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca 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
D:Ca524

b:24.0
occ:1.00
O B:ARG108 2.2 17.0 1.0
OD2 D:ASP357 2.3 19.9 1.0
OE2 B:GLU109 2.5 21.5 1.0
OD2 D:ASP353 2.5 18.1 1.0
OD1 D:ASP353 2.8 18.1 1.0
NZ A:LYS433 2.9 23.5 1.0
OD1 D:ASP357 3.0 19.9 1.0
CG D:ASP353 3.0 18.1 1.0
CG D:ASP357 3.0 19.9 1.0
CD B:GLU109 3.3 21.5 1.0
C B:ARG108 3.4 17.0 1.0
OE1 B:GLU109 3.9 21.5 1.0
CA B:GLU109 4.0 21.5 1.0
N B:GLU109 4.1 21.5 1.0
CD1 A:PHE429 4.2 18.9 1.0
CG B:GLU109 4.2 21.5 1.0
O D:ASP353 4.3 18.1 1.0
CE A:LYS433 4.3 23.5 1.0
CB D:ASP353 4.5 18.1 1.0
CB D:ASP357 4.5 19.9 1.0
CB B:ARG108 4.5 17.0 1.0
CB A:PHE429 4.5 18.9 1.0
CA B:ARG108 4.5 17.0 1.0
CG A:PHE429 4.6 18.9 1.0
CB B:GLU109 4.7 21.5 1.0
C D:ASP353 4.8 18.1 1.0
O B:PHE107 4.9 14.9 1.0
CD A:LYS433 4.9 23.5 1.0
CE1 A:PHE429 4.9 18.9 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: Thu Jul 11 12:40:27 2024

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