Molybdenum in PDB 8dpn: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction:
1.18.6.1;

The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction also contains other interesting chemical elements:

Iron

(Fe)

32 atoms

The binding sites of Molybdenum atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction (pdb code 8dpn). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction, PDB code: 8dpn:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:50.5 occ:1.00 MO1 A:ICS502 0.0 50.5 1.0 S1B A:ICS502 2.3 50.5 1.0 S4B A:ICS502 2.3 50.5 1.0 S3B A:ICS502 2.4 50.5 1.0 ND1 A:HIS442 2.4 24.6 1.0 O7 A:HCA501 2.6 49.1 1.0 FE6 A:ICS502 2.7 50.5 1.0 FE7 A:ICS502 2.7 50.5 1.0 FE5 A:ICS502 2.7 50.5 1.0 O5 A:HCA501 2.7 49.1 1.0 CE1 A:HIS442 3.2 36.8 1.0 CG A:HIS442 3.5 29.6 1.0 CX A:ICS502 3.5 50.5 1.0 C7 A:HCA501 3.6 49.1 1.0 C3 A:HCA501 3.7 49.1 1.0 CB A:HIS442 3.8 37.7 1.0 O1 A:HCA501 4.1 49.1 1.0 C5 A:HCA501 4.3 49.1 1.0 NE2 A:HIS442 4.4 43.3 1.0 CD2 A:HIS442 4.5 36.4 1.0 CA A:HIS442 4.6 30.6 1.0 C4 A:HCA501 4.6 49.1 1.0 C2 A:HCA501 4.7 49.1 1.0 S2B A:ICS502 4.8 50.5 1.0 O6 A:HCA501 4.8 49.1 1.0 S5A A:ICS502 4.8 50.5 1.0 C1 A:HCA501 4.9 49.1 1.0 S3A A:ICS502 4.9 50.5 1.0

Molybdenum binding site 2 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Mofep During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:73.0 occ:1.00 MO1 C:ICS502 0.0 73.0 1.0 S1B C:ICS502 2.3 73.0 1.0 S4B C:ICS502 2.3 73.0 1.0 S3B C:ICS502 2.4 73.0 1.0 ND1 C:HIS442 2.5 26.8 1.0 O7 C:HCA501 2.6 66.0 1.0 FE6 C:ICS502 2.7 73.0 1.0 FE7 C:ICS502 2.7 73.0 1.0 FE5 C:ICS502 2.7 73.0 1.0 O5 C:HCA501 2.7 66.0 1.0 CE1 C:HIS442 3.5 35.2 1.0 CG C:HIS442 3.5 28.5 1.0 CX C:ICS502 3.5 73.0 1.0 C7 C:HCA501 3.6 66.0 1.0 C3 C:HCA501 3.7 66.0 1.0 CB C:HIS442 3.8 36.6 1.0 C5 C:HCA501 4.4 66.0 1.0 CA C:HIS442 4.5 31.4 1.0 O1 C:HCA501 4.5 66.0 1.0 C4 C:HCA501 4.6 66.0 1.0 NE2 C:HIS442 4.6 41.3 1.0 CD2 C:HIS442 4.7 34.5 1.0 C2 C:HCA501 4.7 66.0 1.0 S2B C:ICS502 4.8 73.0 1.0 S5A C:ICS502 4.8 73.0 1.0 O6 C:HCA501 4.8 66.0 1.0 C1 C:HCA501 4.9 66.0 1.0 S3A C:ICS502 4.9 73.0 1.0

H.L.Rutledge, B.D.Cook, H.P.M.Nguyen, M.A.Herzik Jr., F.A.Tezcan. Structures of the Nitrogenase Complex Prepared Under Catalytic Turnover Conditions. Science V. 377 865 2022.
ISSN: ESSN 1095-9203
PubMed: 35901182
DOI: 10.1126/SCIENCE.ABQ7641