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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 8p8g:

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

Chlorine (Cl) 2 atoms
Iron (Fe) 46 atoms
Molybdenum (Mo) 2 atoms

Sodium Binding Sites:

The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G, PDB code: 8p8g:

Sodium binding site 1 out of 1 in 8p8g

Go back to Sodium Binding Sites List in 8p8g
Sodium binding site 1 out of 1 in the Nitrogenase Mofe Protein From A. Vinelandii Beta Double Mutant D353G/D357G


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na 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
C:Na502

b:46.0
occ:1.00
 O C:HOH1077 2.2 46.2 1.0
O C:HOH1030 2.2 35.2 1.0
OD1 C:ASP122 2.8 19.8 1.0
OD2 C:ASP122 3.3 16.2 1.0
CG C:ASP122 3.4 17.9 1.0
NZ C:LYS130 3.4 18.9 1.0
CE C:LYS130 3.7 18.9 1.0
CD C:LYS130 3.9 11.9 1.0
O D:HOH1224 4.5 34.5 1.0
O C:HOH948 4.5 32.6 1.0
O C:HOH879 4.6 24.6 1.0
CG C:LYS130 4.8 14.4 1.0
CB C:ASP122 4.9 15.0 1.0

Reference:

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
Page generated: Wed Oct 9 12:55:11 2024

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