Molybdenum in PDB 7jrf: Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii

All present enzymatic activity of Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii:
1.18.6.1;

The structure of Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 7jrf was solved by T.Spatzal, K.A.Perez, T.M.Buscagan, A.O.Maggiolo, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.63 / 1.33
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	77.052, 129.974, 107.223, 90, 109.11, 90
R / Rfree (%)	11.6 / 15

The structure of Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii also contains other interesting chemical elements:

Iron	(Fe)	30 atoms
Calcium	(Ca)	2 atoms
Magnesium	(Mg)	2 atoms

The binding sites of Molybdenum atom in the Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii (pdb code 7jrf). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii, PDB code: 7jrf:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo502 b:9.8 occ:1.00 MO1 A:ICE502 0.0 9.8 1.0 O6 A:HCA501 2.2 9.1 1.0 O7 A:HCA501 2.2 10.3 1.0 S1B A:ICE502 2.3 10.3 1.0 ND1 A:HIS442 2.3 8.4 1.0 S4B A:ICE502 2.4 9.8 1.0 S3B A:ICE502 2.4 10.0 1.0 FE6 A:ICE502 2.7 10.4 1.0 FE7 A:ICE502 2.7 10.0 1.0 FE5 A:ICE502 2.7 10.1 1.0 C7 A:HCA501 3.0 10.3 1.0 C3 A:HCA501 3.2 10.6 1.0 CE1 A:HIS442 3.3 10.3 1.0 CG A:HIS442 3.4 9.1 1.0 CX A:ICE502 3.5 9.7 1.0 C A:CMO508 3.6 17.8 0.5 CB A:HIS442 3.7 9.6 1.0 C2 A:HCA501 4.1 10.0 1.0 O A:HOH825 4.2 11.8 1.0 O5 A:HCA501 4.2 10.1 1.0 C4 A:HCA501 4.3 10.3 1.0 C5 A:HCA501 4.3 11.1 1.0 O A:CMO508 4.4 20.9 0.5 O2 A:HCA501 4.4 13.8 1.0 NE2 A:HIS442 4.4 10.9 1.0 CD2 A:HIS442 4.5 10.0 1.0 C A:CMO507 4.6 6.4 1.0 CA A:HIS442 4.6 9.8 1.0 S5A A:ICE502 4.8 10.2 1.0 C1 A:HCA501 4.8 12.3 1.0 S3A A:ICE502 4.9 10.1 1.0 FE2 A:ICE502 5.0 10.4 1.0

Molybdenum binding site 2 out of 2 in the Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Co-Co-Bound Nitrogenase Mofe-Protein From A. Vinelandii within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo502 b:10.3 occ:1.00 MO1 C:ICE502 0.0 10.3 1.0 O5 C:HCA501 2.2 10.0 1.0 O7 C:HCA501 2.2 10.6 1.0 S1B C:ICE502 2.3 10.9 1.0 S4B C:ICE502 2.4 10.8 1.0 ND1 C:HIS442 2.4 9.9 1.0 S3B C:ICE502 2.4 10.9 1.0 FE7 C:ICE502 2.7 10.8 1.0 FE6 C:ICE502 2.7 10.9 1.0 FE5 C:ICE502 2.7 10.7 1.0 C7 C:HCA501 3.0 9.7 1.0 C3 C:HCA501 3.2 10.0 1.0 CE1 C:HIS442 3.3 10.7 1.0 CG C:HIS442 3.4 9.7 1.0 C C:CMO506 3.5 17.7 0.5 CX C:ICE502 3.5 9.7 1.0 CB C:HIS442 3.7 10.5 1.0 C2 C:HCA501 4.1 10.6 1.0 O C:HOH760 4.1 12.0 1.0 O6 C:HCA501 4.2 10.7 1.0 C5 C:HCA501 4.2 9.9 1.0 C4 C:HCA501 4.2 10.5 1.0 O C:CMO506 4.4 24.2 0.5 O1 C:HCA501 4.4 14.3 1.0 NE2 C:HIS442 4.5 10.6 1.0 CD2 C:HIS442 4.5 10.5 1.0 CA C:HIS442 4.6 9.4 1.0 C C:CMO505 4.6 5.8 1.0 S5A C:ICE502 4.8 10.9 1.0 C1 C:HCA501 4.8 11.2 1.0 S3A C:ICE502 4.9 11.4 1.0 FE2 C:ICE502 5.0 11.1 1.0

T.M.Buscagan, K.A.Perez, A.O.Maggiolo, D.C.Rees, T.Spatzal. Structural Characterization of Two Co Molecules Bound to the Nitrogenase Active Site. Angew.Chem.Int.Ed.Engl. V. 60 5704 2021.
ISSN: ESSN 1521-3773
PubMed: 33320413
DOI: 10.1002/ANIE.202015751