Chlorine 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:

Sodium	(Na)	1 atom
Iron	(Fe)	46 atoms
Molybdenum	(Mo)	2 atoms

The binding sites of Chlorine 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 Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G, PDB code: 8p8g:
Jump to Chlorine binding site number: 1; 2;

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl1002 b:24.1 occ:1.00 O B:HOH1107 2.7 8.3 1.0 OG1 A:THR111 3.1 15.7 1.0 NH2 A:ARG93 3.3 9.6 1.0 CG B:PHE450 3.4 12.0 1.0 NH1 B:ARG453 3.5 18.3 1.0 CB B:PHE450 3.6 13.3 1.0 NH2 B:ARG453 3.7 18.6 1.0 CD2 B:PHE450 3.7 14.1 1.0 O A:THR111 3.7 14.2 1.0 CG2 A:THR104 3.8 13.4 1.0 CD1 B:PHE450 3.8 17.2 1.0 C A:THR111 3.9 13.5 1.0 CB A:THR111 3.9 15.7 1.0 CG A:MET112 3.9 16.9 1.0 CZ B:ARG453 4.1 17.3 1.0 N A:MET112 4.2 11.7 1.0 CE2 B:PHE450 4.3 15.1 1.0 CE1 B:PHE450 4.4 18.3 1.0 CA A:MET112 4.4 11.4 1.0 CA A:THR111 4.5 14.5 1.0 CZ A:ARG93 4.5 11.1 1.0 O B:HOH816 4.6 19.7 1.0 CZ B:PHE450 4.6 16.7 1.0 CB A:MET112 4.8 13.3 1.0 NE A:ARG93 4.9 11.5 1.0 O A:HOH1333 4.9 22.8 1.0 CB A:THR104 4.9 13.6 1.0

Chlorine 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 Chlorine with other atoms in the Cl 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:Cl501 b:19.0 occ:1.00 O D:HOH1241 2.8 7.2 1.0 OG1 C:THR111 2.9 13.9 1.0 NH1 D:ARG453 3.4 16.0 1.0 NH2 C:ARG93 3.4 11.3 1.0 CG D:PHE450 3.5 10.3 1.0 O C:THR111 3.6 9.4 1.0 NH2 D:ARG453 3.6 14.6 1.0 CG2 C:THR104 3.7 11.2 1.0 CB D:PHE450 3.7 10.4 1.0 C C:THR111 3.7 9.9 1.0 CB C:THR111 3.8 10.4 1.0 CD1 D:PHE450 3.8 11.8 1.0 CD2 D:PHE450 3.8 10.5 1.0 CG C:MET112 3.9 9.9 1.0 CZ D:ARG453 4.0 15.5 1.0 N C:MET112 4.1 8.5 1.0 CA C:THR111 4.3 7.3 1.0 CE1 D:PHE450 4.4 13.9 1.0 CE2 D:PHE450 4.4 12.0 1.0 CA C:MET112 4.5 7.7 1.0 O D:HOH930 4.6 17.5 1.0 CZ C:ARG93 4.6 10.0 1.0 CZ D:PHE450 4.7 10.4 1.0 CB C:THR104 4.8 11.9 1.0 CB C:MET112 4.9 9.3 1.0 O C:HOH951 4.9 18.7 1.0 NE C:ARG93 4.9 7.7 1.0 N C:THR111 4.9 8.1 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