Molybdenum in PDB 7uta: Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction

All present enzymatic activity of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction:
1.18.6.1;

The structure of Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction also contains other interesting chemical elements:

Iron	(Fe)	40 atoms
Magnesium	(Mg)	4 atoms

The binding sites of Molybdenum atom in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction (pdb code 7uta). 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 Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction, PDB code: 7uta:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx 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 Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:53.3 occ:1.00 MO1 A:ICS502 0.0 53.3 1.0 S1B A:ICS502 2.3 53.3 1.0 S4B A:ICS502 2.3 53.3 1.0 S3B A:ICS502 2.4 53.3 1.0 FE6 A:ICS502 2.7 53.3 1.0 FE7 A:ICS502 2.7 53.3 1.0 FE5 A:ICS502 2.7 53.3 1.0 O7 A:HCA501 2.8 55.9 1.0 O5 A:HCA501 2.9 57.1 1.0 ND1 A:HIS442 3.1 54.2 1.0 CX A:ICS502 3.5 53.3 1.0 CG A:HIS442 3.8 55.6 1.0 C7 A:HCA501 3.8 58.7 1.0 C3 A:HCA501 3.9 57.9 1.0 CB A:HIS442 3.9 57.0 1.0 CE1 A:HIS442 4.0 56.2 1.0 O2 A:HCA501 4.1 61.2 1.0 CA A:HIS442 4.5 54.1 1.0 C5 A:HCA501 4.6 59.0 1.0 C1 A:HCA501 4.7 59.8 1.0 S2B A:ICS502 4.8 53.3 1.0 S5A A:ICS502 4.8 53.3 1.0 C4 A:HCA501 4.8 57.6 1.0 C2 A:HCA501 4.9 59.0 1.0 CD2 A:HIS442 4.9 57.8 1.0 NE2 A:HIS442 4.9 59.4 1.0 S3A A:ICS502 4.9 53.3 1.0 O6 A:HCA501 5.0 60.3 1.0

Molybdenum binding site 2 out of 2 in the Cryoem Structure of Azotobacter Vinelandii Nitrogenase Complex (2:1 Fep:Mofep) Inhibited By Befx 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 Complex (2:1 Fep:Mofep) Inhibited By Befx During Catalytic N2 Reduction within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:55.7 occ:1.00 MO1 C:ICS502 0.0 55.7 1.0 S1B C:ICS502 2.3 55.7 1.0 S4B C:ICS502 2.3 55.7 1.0 S3B C:ICS502 2.4 55.7 1.0 FE6 C:ICS502 2.7 55.7 1.0 FE7 C:ICS502 2.7 55.7 1.0 FE5 C:ICS502 2.7 55.7 1.0 O7 C:HCA501 2.9 71.5 1.0 ND1 C:HIS442 2.9 72.0 1.0 O6 C:HCA501 2.9 74.5 1.0 CX C:ICS502 3.5 55.7 1.0 CG C:HIS442 3.7 72.8 1.0 C7 C:HCA501 3.7 73.8 1.0 CB C:HIS442 3.7 73.3 1.0 C3 C:HCA501 3.8 73.0 1.0 CE1 C:HIS442 3.8 73.6 1.0 CA C:HIS442 4.3 72.3 1.0 O2 C:HCA501 4.4 74.2 1.0 C2 C:HCA501 4.4 73.3 1.0 C1 C:HCA501 4.5 73.9 1.0 S2B C:ICS502 4.8 55.7 1.0 CD2 C:HIS442 4.8 75.7 1.0 O5 C:HCA501 4.8 74.3 1.0 S5A C:ICS502 4.8 55.7 1.0 NE2 C:HIS442 4.8 77.0 1.0 O C:HIS442 4.9 75.1 1.0 S3A C:ICS502 4.9 55.7 1.0 O4 C:HCA501 4.9 76.5 1.0 NE C:ARG96 5.0 33.7 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