Iron in PDB 6nh6: Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine

The structure of Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nh6 was solved by G.Chreifi, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	76.41 / 2.19
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.860, 152.820, 109.190, 90.00, 91.00, 90.00
R / Rfree (%)	19.6 / 24.7

The structure of Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Zinc	(Zn)	2 atoms
Gadolinium	(Gd)	4 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Iron atom in the Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine (pdb code 6nh6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nh6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:42.3 occ:1.00 FE A:HEM501 0.0 42.3 1.0 NB A:HEM501 2.1 44.5 1.0 NC A:HEM501 2.1 53.0 1.0 NA A:HEM501 2.1 42.4 1.0 ND A:HEM501 2.1 50.1 1.0 SG A:CYS184 2.3 36.9 1.0 C1B A:HEM501 3.0 45.7 1.0 C4A A:HEM501 3.1 39.2 1.0 C4C A:HEM501 3.1 54.1 1.0 C1D A:HEM501 3.1 61.7 1.0 C1C A:HEM501 3.1 47.7 1.0 C4D A:HEM501 3.1 48.8 1.0 C4B A:HEM501 3.1 46.2 1.0 C1A A:HEM501 3.1 44.4 1.0 CB A:CYS184 3.4 32.6 1.0 CHB A:HEM501 3.4 40.1 1.0 CHD A:HEM501 3.5 53.9 1.0 CHA A:HEM501 3.5 41.8 1.0 CHC A:HEM501 3.5 39.3 1.0 F12 A:KL7503 3.7 53.3 1.0 CA A:CYS184 4.1 33.2 1.0 C03 A:KL7503 4.2 46.4 1.0 C2B A:HEM501 4.3 47.4 1.0 C3B A:HEM501 4.3 39.7 1.0 C3A A:HEM501 4.3 43.4 1.0 C2D A:HEM501 4.3 62.5 1.0 C3D A:HEM501 4.3 62.8 1.0 C3C A:HEM501 4.3 56.3 1.0 C2C A:HEM501 4.3 50.0 1.0 C2A A:HEM501 4.3 54.8 1.0 C04 A:KL7503 4.3 45.4 1.0 NE1 A:TRP178 4.4 50.8 1.0 C07 A:KL7503 4.5 47.9 1.0 C02 A:KL7503 4.7 46.8 1.0 C12 A:KL7503 4.8 61.2 1.0 C13 A:KL7503 4.9 70.0 1.0 C A:CYS184 4.9 36.8 1.0 CD1 A:TRP178 4.9 40.7 1.0

Iron binding site 2 out of 4 in the Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:23.2 occ:1.00 FE B:HEM501 0.0 23.2 1.0 NA B:HEM501 2.0 25.1 1.0 NB B:HEM501 2.1 25.2 1.0 ND B:HEM501 2.1 23.3 1.0 NC B:HEM501 2.1 20.8 1.0 SG B:CYS184 2.4 21.6 1.0 C4A B:HEM501 3.0 23.7 1.0 C1B B:HEM501 3.0 20.8 1.0 C1D B:HEM501 3.1 31.5 1.0 C1A B:HEM501 3.1 18.8 1.0 C1C B:HEM501 3.1 27.9 1.0 C4D B:HEM501 3.1 31.8 1.0 C4B B:HEM501 3.1 28.4 1.0 C4C B:HEM501 3.1 26.3 1.0 CHB B:HEM501 3.4 17.8 1.0 CHC B:HEM501 3.5 22.3 1.0 CHA B:HEM501 3.5 19.0 1.0 CHD B:HEM501 3.5 20.9 1.0 CB B:CYS184 3.5 20.6 1.0 F12 B:KL7503 3.8 53.7 1.0 CA B:CYS184 4.1 20.6 1.0 C2B B:HEM501 4.3 25.2 1.0 C3A B:HEM501 4.3 28.3 1.0 NE1 B:TRP178 4.3 30.0 1.0 C2D B:HEM501 4.3 23.8 1.0 C2A B:HEM501 4.3 38.9 1.0 C3B B:HEM501 4.3 17.8 1.0 C3D B:HEM501 4.3 28.0 1.0 C2C B:HEM501 4.3 28.4 1.0 C03 B:KL7503 4.4 18.5 1.0 C3C B:HEM501 4.4 29.1 1.0 C04 B:KL7503 4.6 26.1 1.0 C02 B:KL7503 4.7 32.5 1.0 C12 B:KL7503 4.8 46.8 1.0 N B:GLY186 4.9 33.3 1.0 C07 B:KL7503 4.9 18.4 1.0 C B:CYS184 4.9 21.0 1.0 CD1 B:TRP178 4.9 21.2 1.0 C13 B:KL7503 4.9 48.2 1.0 N B:VAL185 5.0 27.1 1.0

Iron binding site 3 out of 4 in the Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:31.9 occ:1.00 FE C:HEM501 0.0 31.9 1.0 ND C:HEM501 2.1 35.5 1.0 NA C:HEM501 2.1 35.6 1.0 NC C:HEM501 2.1 47.8 1.0 NB C:HEM501 2.1 30.1 1.0 SG C:CYS184 2.3 32.6 1.0 C4D C:HEM501 3.1 38.3 1.0 C1D C:HEM501 3.1 44.5 1.0 C4A C:HEM501 3.1 36.4 1.0 C1A C:HEM501 3.1 35.5 1.0 C1B C:HEM501 3.1 37.4 1.0 C4C C:HEM501 3.1 42.4 1.0 C1C C:HEM501 3.1 39.6 1.0 C4B C:HEM501 3.1 43.3 1.0 CB C:CYS184 3.3 29.9 1.0 CHA C:HEM501 3.4 33.6 1.0 CHB C:HEM501 3.5 30.8 1.0 CHD C:HEM501 3.5 31.7 1.0 CHC C:HEM501 3.5 36.5 1.0 F12 C:KL7503 3.9 62.5 1.0 CA C:CYS184 4.0 27.8 1.0 C2B C:HEM501 4.3 33.5 1.0 C2D C:HEM501 4.3 36.1 1.0 C3D C:HEM501 4.3 44.7 1.0 C3A C:HEM501 4.3 39.0 1.0 C3B C:HEM501 4.3 38.0 1.0 C2A C:HEM501 4.3 49.4 1.0 C2C C:HEM501 4.4 42.7 1.0 C3C C:HEM501 4.4 38.1 1.0 C03 C:KL7503 4.4 34.1 1.0 NE1 C:TRP178 4.5 41.9 1.0 C04 C:KL7503 4.6 38.7 1.0 C C:CYS184 4.8 26.2 1.0 N C:GLY186 4.8 31.1 1.0 C07 C:KL7503 4.8 38.3 1.0 C02 C:KL7503 4.8 41.0 1.0 N C:VAL185 4.9 26.5 1.0 C12 C:KL7503 5.0 56.5 1.0

Iron binding site 4 out of 4 in the Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of the Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,6- Difluorophenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe501 b:25.5 occ:1.00 FE D:HEM501 0.0 25.5 1.0 NA D:HEM501 2.1 27.4 1.0 NB D:HEM501 2.1 24.9 1.0 NC D:HEM501 2.1 22.1 1.0 ND D:HEM501 2.1 29.2 1.0 SG D:CYS184 2.3 18.9 1.0 C4A D:HEM501 3.0 22.4 1.0 C1B D:HEM501 3.0 27.6 1.0 C4B D:HEM501 3.1 25.2 1.0 C1C D:HEM501 3.1 26.8 1.0 C1A D:HEM501 3.1 29.1 1.0 C1D D:HEM501 3.1 31.9 1.0 C4D D:HEM501 3.1 26.9 1.0 C4C D:HEM501 3.1 27.0 1.0 CB D:CYS184 3.3 18.6 1.0 CHB D:HEM501 3.4 19.9 1.0 CHC D:HEM501 3.5 25.9 1.0 CHA D:HEM501 3.5 25.7 1.0 CHD D:HEM501 3.5 25.6 1.0 F12 D:KL7503 3.6 57.9 1.0 CA D:CYS184 4.0 19.8 1.0 C2B D:HEM501 4.2 32.4 1.0 C3A D:HEM501 4.2 37.2 1.0 C3B D:HEM501 4.3 37.2 1.0 C2A D:HEM501 4.3 41.6 1.0 C2C D:HEM501 4.3 28.8 1.0 C2D D:HEM501 4.3 23.9 1.0 C3D D:HEM501 4.3 34.9 1.0 C03 D:KL7503 4.3 22.2 1.0 C3C D:HEM501 4.4 29.0 1.0 NE1 D:TRP178 4.4 24.3 1.0 C04 D:KL7503 4.6 27.5 1.0 C02 D:KL7503 4.8 26.7 1.0 C12 D:KL7503 4.8 44.9 1.0 C07 D:KL7503 4.8 23.0 1.0 C D:CYS184 4.8 18.9 1.0 N D:GLY186 4.8 22.1 1.0 N D:VAL185 5.0 23.4 1.0

H.T.Do, H.Li, G.Chreifi, T.L.Poulos, R.B.Silverman. Optimization of Blood-Brain Barrier Permeability with Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibitors Having A 2-Aminopyridine Scaffold. J. Med. Chem. V. 62 2690 2019.
ISSN: ISSN 1520-4804
PubMed: 30802056
DOI: 10.1021/ACS.JMEDCHEM.8B02032