Vanadium in PDB 7aiz: Vanadium Nitrogenase Vfe Protein, High Co State

All present enzymatic activity of Vanadium Nitrogenase Vfe Protein, High Co State:
1.18.6.1;

The structure of Vanadium Nitrogenase Vfe Protein, High Co State, PDB code: 7aiz was solved by M.Rohde, O.Einsle, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.39 / 1.05
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	75.521, 80.041, 107.21, 84, 72.48, 75.03
R / Rfree (%)	12.4 / 14.6

The structure of Vanadium Nitrogenase Vfe Protein, High Co State also contains other interesting chemical elements:

Magnesium	(Mg)	4 atoms
Iron	(Fe)	32 atoms

The binding sites of Vanadium atom in the Vanadium Nitrogenase Vfe Protein, High Co State (pdb code 7aiz). This binding sites where shown within 5.0 Angstroms radius around Vanadium atom.
In total 2 binding sites of Vanadium where determined in the Vanadium Nitrogenase Vfe Protein, High Co State, PDB code: 7aiz:
Jump to Vanadium binding site number: 1; 2;

Vanadium binding site 1 out of 2 in the Vanadium Nitrogenase Vfe Protein, High Co State


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 1 of Vanadium Nitrogenase Vfe Protein, High Co State within 5.0Å range: probe atom residue distance (Å) B Occ A:V501 b:8.9 occ:1.00 V1 A:D6N501 0.0 8.9 1.0 O5 A:HCA502 2.1 8.7 1.0 O7 A:HCA502 2.1 8.9 1.0 ND1 A:HIS423 2.3 8.9 1.0 S4B A:D6N501 2.3 9.2 1.0 S1B A:D6N501 2.4 9.4 1.0 S3B A:D6N501 2.4 9.8 1.0 FE5 A:D6N501 2.7 9.2 1.0 FE7 A:D6N501 2.7 9.3 1.0 FE6 A:D6N501 2.8 9.7 1.0 C7 A:HCA502 3.0 9.2 1.0 C3 A:HCA502 3.1 9.0 1.0 CE1 A:HIS423 3.2 9.7 1.0 CG A:HIS423 3.4 9.3 1.0 CX A:D6N501 3.6 9.7 1.0 C A:CMO505 3.8 11.9 0.5 CB A:HIS423 3.8 9.2 1.0 C2 A:HCA502 4.0 9.7 1.0 O A:HOH836 4.2 11.0 1.0 O6 A:HCA502 4.2 9.7 1.0 C4 A:HCA502 4.3 9.3 1.0 O2 A:BCT503 4.3 9.8 1.0 C5 A:HCA502 4.4 9.7 1.0 NE2 A:HIS423 4.4 10.0 1.0 O1 A:HCA502 4.4 10.8 1.0 CD2 A:HIS423 4.5 9.3 1.0 CA A:HIS423 4.5 9.0 1.0 O A:CMO505 4.7 12.8 0.5 NZ A:LYS83 4.7 10.6 1.0 C A:CMO504 4.8 9.2 1.0 C1 A:HCA502 4.8 10.2 1.0 S5A A:D6N501 4.9 9.7 1.0

Vanadium binding site 2 out of 2 in the Vanadium Nitrogenase Vfe Protein, High Co State


Mono view


Stereo pair view

A full contact list of Vanadium with other atoms in the V binding site number 2 of Vanadium Nitrogenase Vfe Protein, High Co State within 5.0Å range: probe atom residue distance (Å) B Occ D:V501 b:8.1 occ:1.00 V1 D:D6N501 0.0 8.1 1.0 O6 D:HCA502 2.1 7.9 1.0 O7 D:HCA502 2.2 8.1 1.0 ND1 D:HIS423 2.3 8.3 1.0 S4B D:D6N501 2.3 8.5 1.0 S1B D:D6N501 2.3 8.4 1.0 S3B D:D6N501 2.4 8.8 1.0 FE5 D:D6N501 2.7 8.5 1.0 FE7 D:D6N501 2.7 8.4 1.0 FE6 D:D6N501 2.8 8.6 1.0 C7 D:HCA502 3.0 8.6 1.0 C3 D:HCA502 3.1 8.0 1.0 CE1 D:HIS423 3.2 8.7 1.0 CG D:HIS423 3.4 8.3 1.0 CX D:D6N501 3.5 8.0 1.0 C D:CMO505 3.7 8.8 0.5 CB D:HIS423 3.8 8.4 1.0 C2 D:HCA502 4.0 8.3 1.0 O D:HOH847 4.2 9.8 1.0 O5 D:HCA502 4.2 8.8 1.0 O1 D:BCT503 4.3 8.7 1.0 C4 D:HCA502 4.3 8.1 1.0 C5 D:HCA502 4.4 8.7 1.0 NE2 D:HIS423 4.4 9.1 1.0 O2 D:HCA502 4.4 10.0 1.0 CD2 D:HIS423 4.5 8.9 1.0 O D:CMO505 4.5 11.3 0.5 CA D:HIS423 4.5 8.4 1.0 NZ D:LYS83 4.7 10.5 1.0 C D:CMO504 4.8 7.5 1.0 C1 D:HCA502 4.8 8.5 1.0 S5A D:D6N501 4.9 8.9 1.0

M.Rohde, K.Laun, I.Zebger, S.T.Stripp, O.Einsle. Two Ligand-Binding Sites in Co-Reducing V Nitrogenase Reveal A General Mechanistic Principle Sci Adv 2021.
ISSN: ESSN 2375-2548
DOI: 10.1126/SCIADV.ABG4474