Molybdenum in PDB 6o7n: Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State

All present enzymatic activity of Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State:
1.18.6.1;

The structure of Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State, PDB code: 6o7n was solved by H.L.Rutledge, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.10 / 1.75
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	76.337, 127.960, 107.509, 90.00, 109.01, 90.00
R / Rfree (%)	18.7 / 22.3

The structure of Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State also contains other interesting chemical elements:

Iron

(Fe)

32 atoms

The binding sites of Molybdenum atom in the Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State (pdb code 6o7n). 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 Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State, PDB code: 6o7n:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:16.6 occ:1.00 MO1 A:ICS502 0.0 16.6 1.0 O7 A:HCA501 2.2 18.5 1.0 O6 A:HCA501 2.3 15.8 1.0 S1B A:ICS502 2.3 15.6 1.0 S4B A:ICS502 2.3 16.9 1.0 S3B A:ICS502 2.4 13.6 1.0 ND1 A:HIS442 2.5 18.2 1.0 FE6 A:ICS502 2.6 17.1 1.0 FE7 A:ICS502 2.7 17.7 1.0 FE5 A:ICS502 2.7 17.4 1.0 HB3 A:HIS442 3.1 22.3 1.0 C7 A:HCA501 3.1 16.4 1.0 C3 A:HCA501 3.2 17.6 1.0 H52 A:HCA501 3.3 21.9 1.0 CE1 A:HIS442 3.4 17.3 1.0 CG A:HIS442 3.5 16.4 1.0 HE1 A:HIS442 3.5 20.7 1.0 CX A:ICS502 3.5 16.4 1.0 CB A:HIS442 3.8 18.6 1.0 H22 A:HCA501 3.9 21.8 1.0 C2 A:HCA501 4.1 18.1 1.0 C5 A:HCA501 4.2 18.2 1.0 O A:HOH729 4.2 18.0 1.0 HA A:HIS442 4.2 21.6 1.0 C4 A:HCA501 4.3 19.7 1.0 O5 A:HCA501 4.3 19.1 1.0 O2 A:HCA501 4.3 21.4 1.0 H51 A:HCA501 4.4 21.9 1.0 HB2 A:HIS442 4.5 22.3 1.0 HG22 A:ILE355 4.5 21.7 1.0 NE2 A:HIS442 4.6 19.2 1.0 CA A:HIS442 4.6 18.0 1.0 HE A:ARG96 4.6 23.8 1.0 CD2 A:HIS442 4.6 17.3 1.0 H41 A:HCA501 4.7 23.7 1.0 S2B A:ICS502 4.7 15.9 1.0 C1 A:HCA501 4.8 22.2 1.0 S5A A:ICS502 4.8 15.9 1.0 HA3 A:GLY356 4.8 24.4 1.0 S3A A:ICS502 4.9 19.4 1.0 FE3 A:ICS502 5.0 17.2 1.0

Molybdenum binding site 2 out of 2 in the Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mofep Mutant F99Y/S188A From Azotobacter Vinelandii in the Indigo Carmine Oxidized State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:15.5 occ:1.00 MO1 C:ICS502 0.0 15.5 1.0 O5 C:HCA501 2.2 17.9 1.0 O7 C:HCA501 2.3 20.2 1.0 S4B C:ICS502 2.3 18.9 1.0 S1B C:ICS502 2.3 15.8 1.0 S3B C:ICS502 2.4 17.0 1.0 ND1 C:HIS442 2.4 20.6 1.0 FE7 C:ICS502 2.7 18.9 1.0 FE6 C:ICS502 2.7 16.3 1.0 FE5 C:ICS502 2.7 19.1 1.0 C7 C:HCA501 3.0 18.5 1.0 HB3 C:HIS442 3.1 22.9 1.0 C3 C:HCA501 3.2 20.1 1.0 CE1 C:HIS442 3.3 19.9 1.0 HE1 C:HIS442 3.3 23.8 1.0 H52 C:HCA501 3.4 24.7 1.0 CG C:HIS442 3.4 17.7 1.0 CX C:ICS502 3.5 19.5 1.0 CB C:HIS442 3.8 19.1 1.0 H22 C:HCA501 4.0 22.1 1.0 C2 C:HCA501 4.2 18.5 1.0 C5 C:HCA501 4.2 20.6 1.0 O1 C:HCA501 4.2 22.8 1.0 HA C:HIS442 4.2 18.9 1.0 O C:HOH843 4.2 20.0 1.0 O6 C:HCA501 4.2 18.4 1.0 H51 C:HCA501 4.3 24.7 1.0 C4 C:HCA501 4.3 20.3 1.0 NE2 C:HIS442 4.4 20.3 1.0 HE C:ARG96 4.5 25.5 1.0 HB2 C:HIS442 4.5 22.9 1.0 CD2 C:HIS442 4.5 18.2 1.0 HG22 C:ILE355 4.6 23.4 1.0 CA C:HIS442 4.6 15.8 1.0 C1 C:HCA501 4.7 22.5 1.0 S5A C:ICS502 4.7 16.7 1.0 H41 C:HCA501 4.8 24.3 1.0 S2B C:ICS502 4.8 15.7 1.0 HA3 C:GLY356 4.9 24.4 1.0 S3A C:ICS502 5.0 20.6 1.0

H.L.Rutledge, J.Rittle, L.M.Williamson, W.A.Xu, D.M.Gagnon, F.A.Tezcan. Redox-Dependent Metastability of the Nitrogenase P-Cluster. J.Am.Chem.Soc. V. 141 10091 2019.
ISSN: ESSN 1520-5126
PubMed: 31146522
DOI: 10.1021/JACS.9B04555