Molybdenum in PDB 5koh: Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced State

All present enzymatic activity of Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced State:
1.18.6.1;

The structure of Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced State, PDB code: 5koh was solved by C.P.Owens, F.A.Tezcan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	143.26 / 1.83
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	202.598, 202.598, 132.567, 90.00, 90.00, 90.00
R / Rfree (%)	12.9 / 15

The structure of Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced State also contains other interesting chemical elements:

Iron

(Fe)

32 atoms

The binding sites of Molybdenum atom in the Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced State (pdb code 5koh). 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 From Gluconacetobacter Diazotrophicus in Dithionite Reduced State, PDB code: 5koh:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced 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 From Gluconacetobacter Diazotrophicus in Dithionite Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:10.4 occ:1.00 MO1 A:ICS502 0.0 10.4 1.0 O7 A:HCA501 2.1 9.5 1.0 O6 A:HCA501 2.1 10.8 1.0 S3B A:ICS502 2.3 10.6 1.0 S1B A:ICS502 2.3 10.4 1.0 ND1 A:HIS458 2.4 9.5 1.0 S4B A:ICS502 2.4 9.8 1.0 FE6 A:ICS502 2.6 11.0 1.0 FE7 A:ICS502 2.7 10.8 1.0 FE5 A:ICS502 2.7 11.0 1.0 C7 A:HCA501 3.0 10.7 1.0 C3 A:HCA501 3.1 10.9 1.0 CE1 A:HIS458 3.2 9.3 1.0 CG A:HIS458 3.4 9.8 1.0 CX A:ICS502 3.5 10.7 1.0 CB A:HIS458 3.7 10.2 1.0 C2 A:HCA501 4.0 11.1 1.0 O A:HOH823 4.1 13.4 1.0 O5 A:HCA501 4.2 10.6 1.0 O2 A:HCA501 4.2 14.5 1.0 C4 A:HCA501 4.2 11.4 1.0 C5 A:HCA501 4.3 12.0 1.0 NE2 A:HIS458 4.4 9.5 1.0 CD2 A:HIS458 4.5 9.5 1.0 CA A:HIS458 4.6 10.5 1.0 C1 A:HCA501 4.7 13.1 1.0 S2B A:ICS502 4.7 12.0 1.0 S5A A:ICS502 4.8 11.9 1.0 S3A A:ICS502 4.9 10.8 1.0

Molybdenum binding site 2 out of 2 in the Nitrogenase Mofep From Gluconacetobacter Diazotrophicus in Dithionite Reduced 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 From Gluconacetobacter Diazotrophicus in Dithionite Reduced State within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:9.8 occ:1.00 MO1 C:ICS502 0.0 9.8 1.0 O7 C:HCA501 2.1 9.2 1.0 O5 C:HCA501 2.2 10.7 1.0 S1B C:ICS502 2.3 10.0 1.0 S4B C:ICS502 2.3 10.0 1.0 S3B C:ICS502 2.3 10.0 1.0 ND1 C:HIS458 2.3 10.1 1.0 FE6 C:ICS502 2.6 10.2 1.0 FE7 C:ICS502 2.7 10.9 1.0 FE5 C:ICS502 2.7 10.3 1.0 C7 C:HCA501 3.0 9.8 1.0 C3 C:HCA501 3.1 11.0 1.0 CE1 C:HIS458 3.2 10.1 1.0 CG C:HIS458 3.4 9.7 1.0 CX C:ICS502 3.5 10.2 1.0 CB C:HIS458 3.7 10.2 1.0 C2 C:HCA501 4.1 11.1 1.0 O C:HOH822 4.1 13.7 1.0 O6 C:HCA501 4.2 8.3 1.0 O1 C:HCA501 4.2 14.6 1.0 C4 C:HCA501 4.2 11.4 1.0 C5 C:HCA501 4.3 11.1 1.0 NE2 C:HIS458 4.4 10.4 1.0 CD2 C:HIS458 4.5 9.7 1.0 CA C:HIS458 4.6 10.2 1.0 C1 C:HCA501 4.7 13.3 1.0 S2B C:ICS502 4.8 10.7 1.0 S5A C:ICS502 4.8 12.2 1.0 S3A C:ICS502 4.9 10.3 1.0

C.P.Owens, F.E.Katz, C.H.Carter, V.F.Oswald, F.A.Tezcan. Tyrosine-Coordinated P-Cluster in G. Diazotrophicus Nitrogenase: Evidence For the Importance of O-Based Ligands in Conformationally Gated Electron Transfer. J.Am.Chem.Soc. V. 138 10124 2016.
ISSN: ESSN 1520-5126
PubMed: 27487256
DOI: 10.1021/JACS.6B06783