Molybdenum in PDB 9ctz: Azotobacter Vinelandii Mofep (C2 Symmetry)

All present enzymatic activity of Azotobacter Vinelandii Mofep (C2 Symmetry):
1.18.6.1;

The structure of Azotobacter Vinelandii Mofep (C2 Symmetry) also contains other interesting chemical elements:

Iron

(Fe)

32 atoms

The binding sites of Molybdenum atom in the Azotobacter Vinelandii Mofep (C2 Symmetry) (pdb code 9ctz). 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 Mofep (C2 Symmetry), PDB code: 9ctz:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Azotobacter Vinelandii Mofep (C2 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 Mofep (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:105.5 occ:1.00 MO1 A:ICS502 0.0 105.5 1.0 S1B A:ICS502 2.3 78.1 1.0 S4B A:ICS502 2.3 84.6 1.0 S3B A:ICS502 2.4 78.1 1.0 FE6 A:ICS502 2.6 88.1 1.0 FE7 A:ICS502 2.6 90.4 1.0 FE5 A:ICS502 2.7 100.3 1.0 O7 A:HCA501 2.7 67.7 1.0 ND1 A:HIS442 2.9 69.0 1.0 O5 A:HCA501 3.0 75.3 1.0 CX A:ICS502 3.5 87.3 1.0 CG A:HIS442 3.7 76.7 1.0 CB A:HIS442 3.8 69.7 1.0 CE1 A:HIS442 3.9 72.6 1.0 C3 A:HCA501 3.9 70.6 1.0 C7 A:HCA501 3.9 72.9 1.0 O A:HOH688 4.3 62.0 1.0 CA A:HIS442 4.5 64.9 1.0 C5 A:HCA501 4.5 69.7 1.0 O1 A:HCA501 4.7 71.8 1.0 S2B A:ICS502 4.7 83.2 1.0 C4 A:HCA501 4.8 66.8 1.0 S5A A:ICS502 4.8 69.3 1.0 S3A A:ICS502 4.9 77.6 1.0 CD2 A:HIS442 4.9 81.2 1.0 C2 A:HCA501 4.9 77.0 1.0 NE2 A:HIS442 4.9 80.5 1.0 FE2 A:ICS502 5.0 83.6 1.0 FE3 A:ICS502 5.0 102.5 1.0

Molybdenum binding site 2 out of 2 in the Azotobacter Vinelandii Mofep (C2 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 Mofep (C2 Symmetry) within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:104.8 occ:1.00 MO1 C:ICS502 0.0 104.8 1.0 S1B C:ICS502 2.3 77.8 1.0 S4B C:ICS502 2.3 85.4 1.0 S3B C:ICS502 2.4 77.4 1.0 FE6 C:ICS502 2.6 90.2 1.0 FE7 C:ICS502 2.6 92.0 1.0 FE5 C:ICS502 2.7 100.0 1.0 O7 C:HCA501 2.7 66.5 1.0 ND1 C:HIS442 2.9 66.2 1.0 O5 C:HCA501 3.0 76.0 1.0 CX C:ICS502 3.5 88.7 1.0 CG C:HIS442 3.7 76.0 1.0 CB C:HIS442 3.8 69.9 1.0 CE1 C:HIS442 3.9 70.0 1.0 C3 C:HCA501 3.9 70.0 1.0 C7 C:HCA501 3.9 73.1 1.0 O C:HOH681 4.2 62.2 1.0 CA C:HIS442 4.5 65.9 1.0 C5 C:HCA501 4.6 69.0 1.0 O1 C:HCA501 4.7 70.9 1.0 S2B C:ICS502 4.7 83.9 1.0 S5A C:ICS502 4.8 70.2 1.0 C4 C:HCA501 4.8 67.4 1.0 S3A C:ICS502 4.9 77.9 1.0 CD2 C:HIS442 4.9 79.9 1.0 NE2 C:HIS442 4.9 78.5 1.0 C2 C:HCA501 4.9 76.1 1.0 FE2 C:ICS502 5.0 80.6 1.0 FE3 C:ICS502 5.0 106.0 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