Fluorine in PDB 6nh1: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh1 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)	38.99 / 2.22
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.264, 152.461, 108.816, 90.00, 90.73, 90.00
R / Rfree (%)	21.2 / 28

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine also contains other interesting chemical elements:

Zinc	(Zn)	4 atoms
Iron	(Fe)	4 atoms
Gadolinium	(Gd)	4 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Fluorine atom in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine (pdb code 6nh1). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 4 binding sites of Fluorine where determined in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh1:
Jump to Fluorine binding site number: 1; 2; 3; 4;

Fluorine binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:F502 b:0.8 occ:1.00 F13 A:KLY502 0.0 0.8 1.0 C13 A:KLY502 1.4 0.2 1.0 C14 A:KLY502 2.3 1.0 1.0 C12 A:KLY502 2.4 0.5 1.0 NE2 A:GLN247 3.5 80.1 1.0 CB A:VAL336 3.6 74.7 1.0 C15 A:KLY502 3.6 0.7 1.0 C11 A:KLY502 3.7 0.1 1.0 O A:SER246 3.7 70.6 1.0 CG A:GLN247 3.8 77.3 1.0 CD A:GLN247 4.1 75.0 1.0 C16 A:KLY502 4.2 0.0 1.0 CG2 A:VAL336 4.2 75.1 1.0 CG1 A:VAL336 4.2 71.2 1.0 C A:SER246 4.3 76.5 1.0 CA A:VAL336 4.4 77.3 1.0 CB A:SER246 4.5 69.7 1.0 OG A:SER246 4.6 77.6 1.0 C17 A:KLY502 4.7 0.5 1.0 OD1 A:ASN338 4.7 0.3 1.0 ND2 A:ASN338 4.8 0.3 1.0 CA A:SER246 4.9 67.5 1.0 C09 A:KLY502 4.9 99.7 1.0 N A:GLN247 5.0 86.6 1.0 CB A:GLN247 5.0 76.8 1.0

Fluorine binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:F504 b:0.6 occ:1.00 F13 B:KLY504 0.0 0.6 1.0 C13 B:KLY504 1.3 0.3 1.0 C14 B:KLY504 2.4 0.6 1.0 C12 B:KLY504 2.4 86.0 1.0 O2D B:HEM502 2.7 65.2 1.0 C15 B:KLY504 3.6 0.7 1.0 C11 B:KLY504 3.6 83.3 1.0 CGD B:HEM502 3.8 65.6 1.0 CBD B:HEM502 4.1 63.1 1.0 C16 B:KLY504 4.1 92.4 1.0 CE1 B:TYR475 4.6 65.1 1.0 C17 B:KLY504 4.6 0.5 1.0 OH B:TYR475 4.8 90.9 1.0 C09 B:KLY504 4.9 65.9 1.0 O1D B:HEM502 4.9 62.7 1.0

Fluorine binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:F503 b:0.8 occ:1.00 F13 C:KLY503 0.0 0.8 1.0 C13 C:KLY503 1.4 0.2 1.0 C14 C:KLY503 2.4 0.4 1.0 C12 C:KLY503 2.4 0.9 1.0 O2D C:HEM501 2.6 94.6 1.0 CGD C:HEM501 3.6 85.5 1.0 C15 C:KLY503 3.6 99.0 1.0 C11 C:KLY503 3.7 97.3 1.0 CBD C:HEM501 3.9 70.4 1.0 C16 C:KLY503 4.2 98.8 1.0 CG1 C:VAL336 4.3 53.4 1.0 CG2 C:VAL336 4.3 60.7 1.0 C17 C:KLY503 4.6 0.5 1.0 O1D C:HEM501 4.7 79.9 1.0 SD C:MET339 4.8 74.5 1.0 C09 C:KLY503 4.9 77.4 1.0 CB C:VAL336 4.9 62.4 1.0 CE1 C:TYR475 5.0 79.7 1.0

Fluorine binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ D:F503 b:0.3 occ:1.00 F13 D:KLY503 0.0 0.3 1.0 C13 D:KLY503 1.3 98.4 1.0 C14 D:KLY503 2.4 91.7 1.0 C12 D:KLY503 2.4 87.8 1.0 O D:HOH611 3.0 52.8 1.0 C15 D:KLY503 3.6 86.4 1.0 C11 D:KLY503 3.7 79.7 1.0 O2D D:HEM501 4.0 60.5 1.0 C16 D:KLY503 4.2 83.2 1.0 NE2 D:GLN247 4.3 67.7 1.0 C17 D:KLY503 4.5 90.0 1.0 CG1 D:VAL336 4.8 41.2 1.0 C09 D:KLY503 4.8 52.0 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