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

Molybdenum Binding Sites:

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

Molybdenum binding site 1 out of 2 in 1n2c

Go back to Molybdenum Binding Sites List in 1n2c
Molybdenum 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 Molybdenum with other atoms in the Mo 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
A:Mo496

b:24.0
occ:1.00
MO1 A:CFM496 0.0 24.0 1.0
O5 A:HCA494 2.2 24.0 1.0
O7 A:HCA494 2.2 24.0 1.0
S3B A:CFM496 2.3 24.0 1.0
ND1 A:HIS442 2.3 19.5 1.0
S4B A:CFM496 2.3 24.0 1.0
S1B A:CFM496 2.4 24.0 1.0
FE6 A:CFM496 2.6 24.0 1.0
FE5 A:CFM496 2.7 24.0 1.0
FE7 A:CFM496 2.7 24.0 1.0
C7 A:HCA494 3.1 24.0 1.0
C3 A:HCA494 3.1 24.0 1.0
CE1 A:HIS442 3.1 19.5 1.0
CG A:HIS442 3.4 19.5 1.0
CB A:HIS442 3.8 19.5 1.0
C2 A:HCA494 4.1 24.0 1.0
C5 A:HCA494 4.1 24.0 1.0
O6 A:HCA494 4.2 24.0 1.0
C4 A:HCA494 4.2 24.0 1.0
NE2 A:HIS442 4.4 19.5 1.0
CA A:HIS442 4.4 19.5 1.0
O1 A:HCA494 4.5 24.0 1.0
CD2 A:HIS442 4.5 19.5 1.0
C1 A:HCA494 4.8 24.0 1.0
S2B A:CFM496 4.8 24.0 1.0
S3A A:CFM496 4.8 24.0 1.0
FE2 A:CFM496 4.8 24.0 1.0
S5 A:CFM496 4.9 24.0 1.0
FE3 A:CFM496 5.0 24.0 1.0
FE4 A:CFM496 5.0 24.0 1.0

Molybdenum binding site 2 out of 2 in 1n2c

Go back to Molybdenum Binding Sites List in 1n2c
Molybdenum 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 Molybdenum with other atoms in the Mo 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
C:Mo496

b:24.0
occ:1.00
MO1 C:CFM496 0.0 24.0 1.0
O7 C:HCA494 2.2 24.0 1.0
O5 C:HCA494 2.2 24.0 1.0
ND1 C:HIS442 2.3 26.2 1.0
S1B C:CFM496 2.3 24.0 1.0
S3B C:CFM496 2.3 24.0 1.0
S4B C:CFM496 2.4 24.0 1.0
FE5 C:CFM496 2.6 24.0 1.0
FE6 C:CFM496 2.6 24.0 1.0
FE7 C:CFM496 2.8 24.0 1.0
C7 C:HCA494 3.1 24.0 1.0
CE1 C:HIS442 3.1 26.2 1.0
C3 C:HCA494 3.1 24.0 1.0
CG C:HIS442 3.4 26.2 1.0
CB C:HIS442 3.8 26.2 1.0
C5 C:HCA494 4.1 24.0 1.0
C2 C:HCA494 4.1 24.0 1.0
C4 C:HCA494 4.2 24.0 1.0
O6 C:HCA494 4.2 24.0 1.0
NE2 C:HIS442 4.3 26.2 1.0
CA C:HIS442 4.4 26.2 1.0
O1 C:HCA494 4.5 24.0 1.0
CD2 C:HIS442 4.5 26.2 1.0
S3A C:CFM496 4.7 24.0 1.0
C1 C:HCA494 4.8 24.0 1.0
S2B C:CFM496 4.8 24.0 1.0
FE2 C:CFM496 4.9 24.0 1.0
S5 C:CFM496 5.0 24.0 1.0
FE4 C:CFM496 5.0 24.0 1.0
FE3 C:CFM496 5.0 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 Dec 15 05:16:00 2020

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