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Magnesium in PDB 5jfc: Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus

Enzymatic activity of Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus

All present enzymatic activity of Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus:
1.6.1.4;

Protein crystallography data

The structure of Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus, PDB code: 5jfc was solved by O.A.Zadvornyy, G.J.Schut, D.M.Nguyen, J.H.Artz, M.Tokmina-Lukaszewska, G.Lipscomb, P.W.King, M.W.Adams, J.W.Peters, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.59 / 1.60
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 179.927, 179.927, 80.792, 90.00, 90.00, 120.00
R / Rfree (%) 14.7 / 15.9

Other elements in 5jfc:

The structure of Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus also contains other interesting chemical elements:

Iron (Fe) 10 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus (pdb code 5jfc). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus, PDB code: 5jfc:

Magnesium binding site 1 out of 1 in 5jfc

Go back to Magnesium Binding Sites List in 5jfc
Magnesium binding site 1 out of 1 in the Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Nadh-Dependent Ferredoxin:Nadp Oxidoreductase (Nfni) From Pyrococcus Furiosus within 5.0Å range:
probe atom residue distance (Å) B Occ
S:Mg502

b:8.9
occ:1.00
O1A S:FAD500 1.8 9.7 1.0
OE1 S:GLU49 2.0 9.7 1.0
O S:HOH762 2.1 10.6 1.0
O1P S:FAD500 2.1 8.9 1.0
O S:HOH626 2.1 10.0 1.0
O S:HOH607 2.1 10.2 1.0
CD S:GLU49 3.0 11.4 1.0
PA S:FAD500 3.1 10.2 1.0
P S:FAD500 3.2 10.0 1.0
OE2 S:GLU49 3.3 11.2 1.0
O5' S:FAD500 3.5 10.0 1.0
O3P S:FAD500 3.6 9.8 1.0
O2A S:FAD500 4.0 10.2 1.0
OG1 S:THR75 4.0 9.7 1.0
O L:HOH662 4.1 15.9 1.0
O S:HOH666 4.2 11.6 1.0
O5B S:FAD500 4.3 9.5 1.0
O S:HOH667 4.3 12.1 1.0
CG S:GLU49 4.3 9.5 1.0
O S:HOH925 4.4 21.8 1.0
H8A S:FAD500 4.5 14.2 1.0
N7A S:FAD500 4.5 11.0 1.0
CB S:THR75 4.5 8.9 1.0
O2P S:FAD500 4.6 9.2 1.0
N S:THR75 4.6 9.6 1.0
CG S:GLU270 4.7 10.5 1.0
C8A S:FAD500 4.8 11.8 1.0
C5' S:FAD500 4.8 9.4 1.0
H5'2 S:FAD500 4.9 11.3 1.0
O S:HOH743 4.9 10.3 1.0
CG2 S:ILE51 5.0 9.2 1.0

Reference:

C.E.Lubner, D.P.Jennings, D.W.Mulder, G.J.Schut, O.A.Zadvornyy, J.P.Hoben, M.Tokmina-Lukaszewska, L.Berry, D.M.Nguyen, G.L.Lipscomb, B.Bothner, A.K.Jones, A.F.Miller, P.W.King, M.W.W.Adams, J.W.Peters. Mechanistic Insights Into Energy Conservation By Flavin-Based Electron Bifurcation. Nat. Chem. Biol. V. 13 655 2017.
ISSN: ESSN 1552-4469
PubMed: 28394885
DOI: 10.1038/NCHEMBIO.2348
Page generated: Mon Dec 14 20:33:32 2020

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