Molybdenum in PDB 1n2c: 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;

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

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

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 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 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

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