Molybdenum in PDB 8p8g: Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G

All present enzymatic activity of Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G:
1.18.6.1;

The structure of Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G, PDB code: 8p8g was solved by N.Maslac, T.Wagner, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.32 / 1.55
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	167.486, 74.469, 208.467, 90, 103.25, 90
R / Rfree (%)	15.5 / 18.7

The structure of Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G also contains other interesting chemical elements:

Chlorine	(Cl)	2 atoms
Sodium	(Na)	1 atom
Iron	(Fe)	46 atoms

The binding sites of Molybdenum atom in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G (pdb code 8p8g). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G, PDB code: 8p8g:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G within 5.0Å range: probe atom residue distance (Å) B Occ A:Mo1004 b:9.6 occ:1.00 MO1 A:ICS1004 0.0 9.6 1.0 ND1 A:HIS442 2.3 7.4 1.0 S1B A:ICS1004 2.3 6.8 1.0 S3B A:ICS1004 2.3 8.3 1.0 S4B A:ICS1004 2.3 7.3 1.0 O6 A:HCA1003 2.3 8.8 1.0 O7 A:HCA1003 2.4 6.9 1.0 FE6 A:ICS1004 2.6 8.6 1.0 FE5 A:ICS1004 2.7 10.2 1.0 FE7 A:ICS1004 2.7 10.3 1.0 CE1 A:HIS442 3.1 9.2 1.0 C7 A:HCA1003 3.2 11.0 1.0 C3 A:HCA1003 3.3 10.1 1.0 CG A:HIS442 3.4 10.3 1.0 CX A:ICS1004 3.5 8.2 1.0 CB A:HIS442 3.8 11.2 1.0 O A:HOH1309 4.1 14.0 1.0 C5 A:HCA1003 4.2 10.3 1.0 C2 A:HCA1003 4.2 12.1 1.0 C4 A:HCA1003 4.3 10.1 1.0 NE2 A:HIS442 4.3 10.2 1.0 O5 A:HCA1003 4.3 8.7 1.0 CD2 A:HIS442 4.5 9.4 1.0 O2 A:HCA1003 4.5 13.5 1.0 CA A:HIS442 4.6 10.0 1.0 S2B A:ICS1004 4.8 10.1 1.0 S3A A:ICS1004 4.8 10.0 1.0 S5A A:ICS1004 4.8 10.4 1.0 C1 A:HCA1003 4.9 15.0 1.0

Molybdenum binding site 2 out of 2 in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 2 of Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G within 5.0Å range: probe atom residue distance (Å) B Occ C:Mo504 b:7.7 occ:1.00 MO1 C:ICS504 0.0 7.7 1.0 S1B C:ICS504 2.3 6.3 1.0 O5 C:HCA503 2.3 5.8 1.0 S4B C:ICS504 2.3 6.9 1.0 O7 C:HCA503 2.4 6.7 1.0 S3B C:ICS504 2.4 5.8 1.0 ND1 C:HIS442 2.5 7.0 1.0 FE5 C:ICS504 2.7 8.3 1.0 FE7 C:ICS504 2.7 7.4 1.0 FE6 C:ICS504 2.8 6.5 1.0 C7 C:HCA503 3.1 9.1 1.0 C3 C:HCA503 3.3 6.8 1.0 CE1 C:HIS442 3.5 9.9 1.0 CG C:HIS442 3.5 7.0 1.0 CX C:ICS504 3.6 10.5 1.0 CB C:HIS442 3.7 8.2 1.0 C2 C:HCA503 4.2 8.0 1.0 C5 C:HCA503 4.2 11.0 1.0 O C:HOH887 4.3 11.2 1.0 O1 C:HCA503 4.3 7.1 1.0 O6 C:HCA503 4.3 7.7 1.0 C4 C:HCA503 4.3 10.4 1.0 CA C:HIS442 4.6 7.8 1.0 NE2 C:HIS442 4.6 11.9 1.0 CD2 C:HIS442 4.6 8.8 1.0 C1 C:HCA503 4.8 8.0 1.0 S5A C:ICS504 4.8 8.1 1.0 S3A C:ICS504 4.8 7.2 1.0 S2B C:ICS504 4.9 8.8 1.0

C.Cadoux, N.Maslac, L.Di Luzio, D.Ratcliff, W.Gu, T.Wagner, R.D.Milton. The Mononuclear Metal-Binding Site of Mo-Nitrogenase Is Not Required For Activity. Jacs Au V. 3 2993 2023.
ISSN: ESSN 2691-3704
PubMed: 38034976
DOI: 10.1021/JACSAU.3C00567