Molybdenum in PDB 9cu0: Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry):
1.18.6.1;

The structure of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) also contains other interesting chemical elements:

Magnesium	(Mg)	2 atoms
Iron	(Fe)	38 atoms

The binding sites of Molybdenum atom in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) (pdb code 9cu0). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry), PDB code: 9cu0:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:102.6 occ:1.00 MO1 A:ICS502 0.0 102.6 1.0 S1B A:ICS502 2.3 102.6 1.0 S4B A:ICS502 2.3 102.6 1.0 S3B A:ICS502 2.4 102.6 1.0 FE6 A:ICS502 2.6 102.6 1.0 FE7 A:ICS502 2.6 102.6 1.0 FE5 A:ICS502 2.7 102.6 1.0 O7 A:HCA501 2.7 99.6 1.0 O5 A:HCA501 2.9 99.6 1.0 ND1 A:HIS442 3.0 95.7 1.0 CX A:ICS502 3.5 102.6 1.0 C7 A:HCA501 3.5 99.6 1.0 C3 A:HCA501 3.6 99.6 1.0 CG A:HIS442 3.8 95.7 1.0 CE1 A:HIS442 3.9 95.7 1.0 CB A:HIS442 3.9 95.7 1.0 C2 A:HCA501 4.0 99.6 1.0 O1 A:HCA501 4.0 99.6 1.0 C1 A:HCA501 4.5 99.6 1.0 CA A:HIS442 4.6 95.7 1.0 O6 A:HCA501 4.6 99.6 1.0 S2B A:ICS502 4.7 102.6 1.0 S5A A:ICS502 4.8 102.6 1.0 O4 A:HCA501 4.8 99.6 1.0 S3A A:ICS502 4.8 102.6 1.0 FE2 A:ICS502 5.0 102.6 1.0 FE3 A:ICS502 5.0 102.6 1.0 CD2 A:HIS442 5.0 95.7 1.0 C4 A:HCA501 5.0 99.6 1.0 NE2 A:HIS442 5.0 95.7 1.0

Molybdenum binding site 2 out of 2 in the Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry)


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Azotobacter Vinelandii 1:1:1 Mofep:Fep:Fesii-Complex (C1 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:141.6 occ:1.00 MO1 C:ICS502 0.0 141.6 1.0 O7 C:HCA501 2.0 118.5 1.0 S4B C:ICS502 2.4 141.6 1.0 S1B C:ICS502 2.4 141.6 1.0 S3B C:ICS502 2.4 141.6 1.0 FE6 C:ICS502 2.7 141.6 1.0 FE7 C:ICS502 2.7 141.6 1.0 FE5 C:ICS502 2.7 141.6 1.0 O5 C:HCA501 3.1 118.5 1.0 ND1 C:HIS442 3.1 120.3 1.0 C3 C:HCA501 3.3 118.5 1.0 C7 C:HCA501 3.5 118.5 1.0 CX C:ICS502 3.6 141.6 1.0 CG C:HIS442 3.8 120.3 1.0 CE1 C:HIS442 3.9 120.3 1.0 O1 C:HCA501 3.9 118.5 1.0 CB C:HIS442 4.0 120.3 1.0 C2 C:HCA501 4.1 118.5 1.0 C4 C:HCA501 4.2 118.5 1.0 C1 C:HCA501 4.3 118.5 1.0 CA C:HIS442 4.5 120.3 1.0 O6 C:HCA501 4.7 118.5 1.0 O C:HIS442 4.7 120.3 1.0 S2B C:ICS502 4.8 141.6 1.0 S5A C:ICS502 4.8 141.6 1.0 CD2 C:HIS442 4.9 120.3 1.0 S3A C:ICS502 4.9 141.6 1.0 NE2 C:HIS442 4.9 120.3 1.0 C C:HIS442 5.0 120.3 1.0

S.M.Narehood, B.D.Cook, S.Srisantitham, V.H.Eng, A.Shiau, K.L.Mcguire, R.D.Britt, M.A.Herzik, F.A.Tezcan. Structural Basis For the Conformational Protection of Nitrogenase From O2 Nature 2025.
ISSN: ESSN 1476-4687
DOI: 10.1038/S41586-024-08311-1