Iron in PDB 6nh7: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nh7 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)	76.74 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.959, 109.381, 153.470, 90.00, 90.00, 90.00
R / Rfree (%)	21 / 25.8

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine also contains other interesting chemical elements:

Fluorine	(F)	12 atoms
Zinc	(Zn)	1 atom
Gadolinium	(Gd)	4 atoms

The binding sites of Iron atom in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine (pdb code 6nh7). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nh7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:33.4 occ:1.00 FE A:HEM501 0.0 33.4 1.0 ND A:HEM501 2.0 42.2 1.0 NA A:HEM501 2.1 43.2 1.0 NC A:HEM501 2.1 36.5 1.0 NB A:HEM501 2.2 40.6 1.0 SG A:CYS184 2.2 33.5 1.0 C4C A:HEM501 3.0 36.7 1.0 C1D A:HEM501 3.1 49.5 1.0 C4D A:HEM501 3.1 45.8 1.0 C1A A:HEM501 3.1 46.6 1.0 C4A A:HEM501 3.1 42.8 1.0 C1C A:HEM501 3.1 39.3 1.0 C1B A:HEM501 3.1 45.1 1.0 C4B A:HEM501 3.2 43.3 1.0 CB A:CYS184 3.3 35.0 1.0 CHD A:HEM501 3.4 40.4 1.0 CHA A:HEM501 3.4 36.1 1.0 CHB A:HEM501 3.5 35.9 1.0 CHC A:HEM501 3.5 31.7 1.0 C04 A:KMM502 4.1 43.7 1.0 CA A:CYS184 4.1 38.5 1.0 C03 A:KMM502 4.2 38.2 1.0 C3D A:HEM501 4.3 51.4 1.0 C2D A:HEM501 4.3 45.1 1.0 C3C A:HEM501 4.3 34.7 1.0 C2A A:HEM501 4.3 50.2 1.0 C3A A:HEM501 4.3 47.2 1.0 C2C A:HEM501 4.3 35.8 1.0 NE1 A:TRP178 4.3 37.5 1.0 C2B A:HEM501 4.3 40.0 1.0 C3B A:HEM501 4.4 42.8 1.0 C05 A:KMM502 4.4 52.4 1.0 C07 A:KMM502 4.4 37.6 1.0 C02 A:KMM502 4.6 35.4 1.0 C06 A:KMM502 4.8 50.7 1.0 N01 A:KMM502 4.8 38.7 1.0 C A:CYS184 4.9 33.5 1.0 CD1 A:TRP178 5.0 46.2 1.0 N A:GLY186 5.0 28.4 1.0

Iron binding site 2 out of 2 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-(3-(Dimethylamino)Propyl)-2,5,6- Trifluorophenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:32.7 occ:1.00 FE B:HEM501 0.0 32.7 1.0 ND B:HEM501 2.0 26.6 1.0 NB B:HEM501 2.1 30.3 1.0 NA B:HEM501 2.1 31.5 1.0 NC B:HEM501 2.1 28.1 1.0 SG B:CYS184 2.2 28.2 1.0 C1D B:HEM501 3.0 29.6 1.0 C1B B:HEM501 3.0 29.6 1.0 C4D B:HEM501 3.1 33.9 1.0 C4C B:HEM501 3.1 25.8 1.0 C4A B:HEM501 3.1 30.6 1.0 C4B B:HEM501 3.1 32.1 1.0 C1A B:HEM501 3.1 35.0 1.0 C1C B:HEM501 3.2 25.3 1.0 CHD B:HEM501 3.3 27.9 1.0 CB B:CYS184 3.4 27.9 1.0 CHB B:HEM501 3.4 29.6 1.0 CHA B:HEM501 3.5 26.5 1.0 CHC B:HEM501 3.5 30.0 1.0 C04 B:KMM502 4.1 30.5 1.0 CA B:CYS184 4.1 29.8 1.0 C03 B:KMM502 4.2 30.5 1.0 C2D B:HEM501 4.2 24.5 1.0 C2B B:HEM501 4.2 30.8 1.0 C3D B:HEM501 4.3 29.5 1.0 C3B B:HEM501 4.3 27.5 1.0 C3C B:HEM501 4.3 33.1 1.0 C3A B:HEM501 4.3 30.4 1.0 C2A B:HEM501 4.3 40.0 1.0 C2C B:HEM501 4.4 24.9 1.0 C05 B:KMM502 4.4 34.1 1.0 NE1 B:TRP178 4.4 34.1 1.0 C07 B:KMM502 4.4 25.3 1.0 C02 B:KMM502 4.6 37.3 1.0 C06 B:KMM502 4.8 34.0 1.0 N B:GLY186 4.8 30.4 1.0 N01 B:KMM502 4.8 30.6 1.0 C B:CYS184 4.9 29.6 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