Iron in PDB 6nhf: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nhf 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)	49.50 / 1.83
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.336, 152.557, 108.524, 90.00, 90.70, 90.00
R / Rfree (%)	18.3 / 21.9

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine (pdb code 6nhf). 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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nhf:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-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 (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:40.8 occ:1.00 FE A:HEM501 0.0 40.8 1.0 ND A:HEM501 2.1 46.5 1.0 NA A:HEM501 2.1 44.5 1.0 NB A:HEM501 2.1 42.8 1.0 NC A:HEM501 2.1 44.8 1.0 SG A:CYS184 2.3 39.3 1.0 C4D A:HEM501 3.0 45.5 1.0 C4B A:HEM501 3.1 53.1 1.0 C1D A:HEM501 3.1 51.9 1.0 C1A A:HEM501 3.1 46.2 1.0 C1B A:HEM501 3.1 56.3 1.0 C4A A:HEM501 3.1 51.2 1.0 C1C A:HEM501 3.1 48.3 1.0 C4C A:HEM501 3.1 54.7 1.0 CHA A:HEM501 3.4 37.6 1.0 CHC A:HEM501 3.4 46.5 1.0 CHB A:HEM501 3.5 47.4 1.0 CB A:CYS184 3.5 39.2 1.0 CHD A:HEM501 3.5 52.6 1.0 C04 A:KNV503 3.9 58.1 1.0 C05 A:KNV503 3.9 66.2 1.0 C03 A:KNV503 4.2 52.6 1.0 CA A:CYS184 4.2 35.4 1.0 C06 A:KNV503 4.2 65.4 1.0 C3D A:HEM501 4.3 55.2 1.0 C2D A:HEM501 4.3 52.4 1.0 C2B A:HEM501 4.3 49.3 1.0 C3B A:HEM501 4.3 51.6 1.0 C3A A:HEM501 4.3 48.1 1.0 C07 A:KNV503 4.3 50.5 1.0 C2A A:HEM501 4.3 49.6 1.0 C2C A:HEM501 4.3 47.8 1.0 C3C A:HEM501 4.4 49.9 1.0 NE1 A:TRP178 4.4 46.3 1.0 C02 A:KNV503 4.5 53.5 1.0 N01 A:KNV503 4.5 60.7 1.0 C08 A:KNV503 5.0 79.9 1.0 C A:CYS184 5.0 38.2 1.0 N A:GLY186 5.0 44.5 1.0

Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-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 (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe501 b:30.4 occ:1.00 FE B:HEM501 0.0 30.4 1.0 NB B:HEM501 2.0 29.3 1.0 ND B:HEM501 2.0 28.1 1.0 NC B:HEM501 2.1 25.4 1.0 NA B:HEM501 2.1 34.0 1.0 SG B:CYS184 2.3 28.0 1.0 C4B B:HEM501 3.0 32.0 1.0 C1B B:HEM501 3.1 31.3 1.0 C1D B:HEM501 3.1 27.1 1.0 C4D B:HEM501 3.1 33.2 1.0 C4A B:HEM501 3.1 30.4 1.0 C1C B:HEM501 3.1 25.0 1.0 C4C B:HEM501 3.1 24.8 1.0 C1A B:HEM501 3.1 24.3 1.0 CB B:CYS184 3.4 23.5 1.0 CHC B:HEM501 3.4 32.8 1.0 CHB B:HEM501 3.4 31.6 1.0 CHD B:HEM501 3.5 28.4 1.0 CHA B:HEM501 3.5 25.2 1.0 C04 B:KNV503 4.1 40.4 1.0 CA B:CYS184 4.1 28.7 1.0 C05 B:KNV503 4.2 42.7 1.0 C3B B:HEM501 4.2 27.0 1.0 C2B B:HEM501 4.2 32.6 1.0 C2D B:HEM501 4.3 29.4 1.0 C3D B:HEM501 4.3 32.4 1.0 C03 B:KNV503 4.3 33.4 1.0 C3A B:HEM501 4.3 29.4 1.0 NE1 B:TRP178 4.3 30.2 1.0 C2C B:HEM501 4.3 25.6 1.0 C2A B:HEM501 4.3 32.3 1.0 C3C B:HEM501 4.3 23.1 1.0 C06 B:KNV503 4.5 53.8 1.0 C07 B:KNV503 4.5 35.0 1.0 C02 B:KNV503 4.6 33.8 1.0 N01 B:KNV503 4.6 36.7 1.0 N B:GLY186 4.8 31.1 1.0 C B:CYS184 4.9 26.9 1.0 CD1 B:TRP178 5.0 26.6 1.0

Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe501 b:37.8 occ:1.00 FE C:HEM501 0.0 37.8 1.0 NB C:HEM501 2.1 42.8 1.0 ND C:HEM501 2.1 41.3 1.0 NC C:HEM501 2.1 39.0 1.0 NA C:HEM501 2.1 36.1 1.0 SG C:CYS184 2.3 35.4 1.0 C4B C:HEM501 3.0 46.5 1.0 C1C C:HEM501 3.1 45.5 1.0 C4D C:HEM501 3.1 44.1 1.0 C1B C:HEM501 3.1 41.3 1.0 C1A C:HEM501 3.1 38.8 1.0 C4A C:HEM501 3.1 38.7 1.0 C1D C:HEM501 3.1 43.7 1.0 C4C C:HEM501 3.1 34.2 1.0 CB C:CYS184 3.4 33.5 1.0 CHC C:HEM501 3.4 38.0 1.0 CHA C:HEM501 3.4 32.5 1.0 CHB C:HEM501 3.5 34.7 1.0 CHD C:HEM501 3.5 41.1 1.0 CA C:CYS184 4.0 36.8 1.0 C04 C:KNV503 4.1 59.2 1.0 C05 C:KNV503 4.2 67.6 1.0 C3B C:HEM501 4.3 46.9 1.0 C2B C:HEM501 4.3 38.8 1.0 C3D C:HEM501 4.3 43.1 1.0 C2C C:HEM501 4.3 44.2 1.0 C2D C:HEM501 4.3 39.2 1.0 C3A C:HEM501 4.3 42.8 1.0 C3C C:HEM501 4.3 36.5 1.0 C2A C:HEM501 4.3 44.6 1.0 C03 C:KNV503 4.4 51.4 1.0 C06 C:KNV503 4.4 67.5 1.0 NE1 C:TRP178 4.4 43.6 1.0 C07 C:KNV503 4.6 62.6 1.0 C02 C:KNV503 4.6 49.1 1.0 N01 C:KNV503 4.6 54.0 1.0 C C:CYS184 4.8 33.9 1.0 N C:GLY186 4.8 38.2 1.0 N C:VAL185 5.0 29.5 1.0

Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe501 b:28.4 occ:1.00 FE D:HEM501 0.0 28.4 1.0 ND D:HEM501 2.0 29.8 1.0 NA D:HEM501 2.1 26.7 1.0 NC D:HEM501 2.1 24.7 1.0 NB D:HEM501 2.1 27.8 1.0 SG D:CYS184 2.3 27.6 1.0 C1D D:HEM501 3.0 30.2 1.0 C4A D:HEM501 3.1 27.0 1.0 C4C D:HEM501 3.1 27.9 1.0 C4D D:HEM501 3.1 30.8 1.0 C1B D:HEM501 3.1 29.9 1.0 C1A D:HEM501 3.1 31.6 1.0 C4B D:HEM501 3.1 29.6 1.0 C1C D:HEM501 3.1 29.2 1.0 CB D:CYS184 3.3 24.4 1.0 CHD D:HEM501 3.4 33.0 1.0 CHB D:HEM501 3.4 30.2 1.0 CHA D:HEM501 3.5 28.4 1.0 CHC D:HEM501 3.5 30.3 1.0 CA D:CYS184 4.0 23.0 1.0 C04 D:KNV503 4.2 39.2 1.0 C2D D:HEM501 4.3 29.8 1.0 C3D D:HEM501 4.3 33.5 1.0 C3A D:HEM501 4.3 32.8 1.0 C3C D:HEM501 4.3 27.4 1.0 C2A D:HEM501 4.3 35.3 1.0 C05 D:KNV503 4.3 44.0 1.0 C2C D:HEM501 4.3 25.9 1.0 C2B D:HEM501 4.3 29.4 1.0 C3B D:HEM501 4.4 27.8 1.0 C03 D:KNV503 4.4 34.7 1.0 NE1 D:TRP178 4.4 28.6 1.0 C07 D:KNV503 4.6 37.3 1.0 C06 D:KNV503 4.6 53.8 1.0 C02 D:KNV503 4.7 35.7 1.0 N D:GLY186 4.8 26.8 1.0 N01 D:KNV503 4.8 32.3 1.0 C D:CYS184 4.8 28.6 1.0 N D:VAL185 5.0 28.2 1.0 CD1 D:TRP178 5.0 26.7 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