Fluorine in PDB 6nh2: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh2 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)	88.89 / 2.29
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	60.329, 153.769, 108.939, 90.00, 90.86, 90.00
R / Rfree (%)	17.3 / 22.2

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

Zinc	(Zn)	6 atoms
Iron	(Fe)	4 atoms
Gadolinium	(Gd)	2 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 (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine (pdb code 6nh2). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 6 binding sites of Fluorine where determined in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh2:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6;

Fluorine binding site 1 out of 6 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)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 (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:F503 b:61.9 occ:1.00 F13 A:KMA503 0.0 61.9 1.0 C13 A:KMA503 1.3 66.8 1.0 C14 A:KMA503 2.3 67.0 1.0 C12 A:KMA503 2.4 66.9 1.0 O1A A:HEM501 2.6 70.9 1.0 O4 A:H4B502 3.3 91.2 1.0 NH1 A:ARG365 3.4 48.9 1.0 N3 A:H4B502 3.4 78.1 1.0 CZ A:ARG365 3.4 49.4 1.0 NE A:ARG365 3.5 51.8 1.0 CZ3 A:TRP447 3.5 38.6 1.0 CGA A:HEM501 3.6 66.2 1.0 C15 A:KMA503 3.6 66.9 1.0 CD A:ARG365 3.6 51.8 1.0 C11 A:KMA503 3.7 59.0 1.0 C4 A:H4B502 3.7 81.6 1.0 CH2 A:TRP447 4.0 35.6 1.0 NH2 A:ARG365 4.0 42.8 1.0 C16 A:KMA503 4.1 64.1 1.0 O2A A:HEM501 4.3 67.2 1.0 CE3 A:TRP447 4.4 30.7 1.0 O A:HOH744 4.4 48.5 1.0 O A:HOH722 4.5 52.1 1.0 CAA A:HEM501 4.5 37.0 1.0 C2 A:H4B502 4.5 81.8 1.0 CBA A:HEM501 4.5 53.1 1.0 C17 A:KMA503 4.8 66.4 1.0 N2 A:H4B502 4.9 79.1 1.0 C09 A:KMA503 4.9 50.0 1.0

Fluorine binding site 2 out of 6 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)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 (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:F509 b:60.0 occ:1.00 F13 A:KMA509 0.0 60.0 1.0 C13 A:KMA509 1.3 59.6 1.0 C14 A:KMA509 2.3 62.1 1.0 C12 A:KMA509 2.4 63.3 1.0 O B:HOH679 3.3 33.6 1.0 O B:HOH763 3.3 44.5 1.0 C14 B:KMA502 3.4 65.1 1.0 C15 A:KMA509 3.6 66.0 1.0 CD B:ARG365 3.6 34.3 1.0 C11 A:KMA509 3.6 58.8 1.0 O B:HOH766 3.9 16.2 1.0 C15 B:KMA502 4.1 66.1 1.0 C13 B:KMA502 4.1 61.7 1.0 NH1 B:ARG372 4.1 21.3 1.0 C16 A:KMA509 4.1 61.1 1.0 O B:HOH661 4.1 42.8 1.0 C17 B:KMA502 4.1 71.5 1.0 F13 B:KMA502 4.1 53.8 1.0 NE B:ARG365 4.3 38.6 1.0 CG B:ARG365 4.5 29.1 1.0 C23 B:KMA502 4.5 69.6 1.0 O B:HOH719 4.5 32.2 1.0 C17 A:KMA509 4.9 71.7 1.0 C09 A:KMA509 4.9 53.5 1.0

Fluorine binding site 3 out of 6 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)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 (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:F502 b:53.8 occ:1.00 F13 B:KMA502 0.0 53.8 1.0 C13 B:KMA502 1.3 61.7 1.0 C14 B:KMA502 2.3 65.1 1.0 C12 B:KMA502 2.4 62.1 1.0 NE B:ARG365 3.3 38.6 1.0 NH2 B:ARG365 3.4 50.6 1.0 CZ B:ARG365 3.5 38.4 1.0 O1A B:HEM501 3.6 75.1 1.0 CZ3 B:TRP447 3.6 31.6 1.0 C15 B:KMA502 3.6 66.1 1.0 C11 B:KMA502 3.7 61.6 1.0 C12 A:KMA509 4.0 63.3 1.0 O B:HOH773 4.0 27.2 1.0 CH2 B:TRP447 4.0 35.8 1.0 C16 B:KMA502 4.1 64.7 1.0 CGA B:HEM501 4.1 66.2 1.0 F13 A:KMA509 4.1 60.0 1.0 CD B:ARG365 4.2 34.3 1.0 NH1 B:ARG365 4.3 31.2 1.0 CE3 B:TRP447 4.3 26.5 1.0 C13 A:KMA509 4.4 59.6 1.0 CAA B:HEM501 4.6 24.7 1.0 CBA B:HEM501 4.7 46.6 1.0 O2A B:HEM501 4.8 67.2 1.0 C17 B:KMA502 4.9 71.5 1.0 C09 B:KMA502 4.9 51.1 1.0 C11 A:KMA509 4.9 58.8 1.0

Fluorine binding site 4 out of 6 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)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 (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:F504 b:46.3 occ:1.00 F13 C:KMA504 0.0 46.3 1.0 C13 C:KMA504 1.3 53.5 1.0 C14 C:KMA504 2.3 60.4 1.0 C12 C:KMA504 2.4 55.8 1.0 N3 C:H4B503 2.9 78.6 1.0 O4 C:H4B503 3.1 80.9 1.0 NH1 C:ARG365 3.2 76.5 1.0 O2A C:HEM502 3.4 78.2 1.0 CZ C:ARG365 3.4 61.4 1.0 CBA C:HEM502 3.4 66.5 1.0 C4 C:H4B503 3.4 77.9 1.0 NE C:ARG365 3.5 61.9 1.0 CD C:ARG365 3.6 58.7 1.0 C15 C:KMA504 3.6 60.5 1.0 C11 C:KMA504 3.7 58.4 1.0 CGA C:HEM502 3.8 77.7 1.0 CZ3 C:TRP447 3.8 42.1 1.0 C2 C:H4B503 4.0 82.0 1.0 NH2 C:ARG365 4.1 47.8 1.0 C16 C:KMA504 4.1 58.6 1.0 CH2 C:TRP447 4.3 43.4 1.0 N2 C:H4B503 4.3 79.8 1.0 O C:HOH720 4.5 61.1 1.0 O C:HOH724 4.6 43.3 1.0 CE3 C:TRP447 4.6 42.0 1.0 CAA C:HEM502 4.6 44.8 1.0 C4A C:H4B503 4.8 78.9 1.0 C17 C:KMA504 4.9 59.9 1.0 O1A C:HEM502 4.9 80.9 1.0 C09 C:KMA504 4.9 51.6 1.0 O C:HOH692 4.9 35.7 1.0

Fluorine binding site 5 out of 6 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)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 5 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:F510 b:53.8 occ:1.00 F13 C:KMA510 0.0 53.8 1.0 C13 C:KMA510 1.3 57.7 1.0 C14 C:KMA510 2.4 60.4 1.0 C12 C:KMA510 2.4 53.2 1.0 O D:HOH730 3.1 26.1 1.0 C14 D:KMA503 3.4 61.1 1.0 O D:HOH780 3.5 34.8 1.0 C15 C:KMA510 3.6 64.4 1.0 C11 C:KMA510 3.6 55.5 1.0 CD D:ARG365 3.7 26.6 1.0 O D:HOH789 3.8 11.5 1.0 C15 D:KMA503 4.1 66.7 1.0 C17 D:KMA503 4.1 71.5 1.0 NH1 D:ARG372 4.1 32.0 1.0 C16 C:KMA510 4.1 58.7 1.0 O D:HOH677 4.1 38.1 1.0 O D:HOH753 4.1 26.3 1.0 C13 D:KMA503 4.2 57.7 1.0 F13 D:KMA503 4.2 53.8 1.0 CG D:ARG365 4.3 19.1 1.0 NE D:ARG365 4.4 31.5 1.0 C23 D:KMA503 4.4 67.5 1.0 C17 C:KMA510 4.9 71.5 1.0 C09 C:KMA510 4.9 54.0 1.0

Fluorine binding site 6 out of 6 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)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 6 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ D:F503 b:53.8 occ:1.00 F13 D:KMA503 0.0 53.8 1.0 C13 D:KMA503 1.3 57.7 1.0 C14 D:KMA503 2.3 61.1 1.0 C12 D:KMA503 2.4 62.4 1.0 CZ3 D:TRP447 3.4 34.7 1.0 O D:HOH830 3.4 38.2 1.0 CBA D:HEM502 3.5 52.9 1.0 NH2 D:ARG365 3.5 48.2 1.0 NE D:ARG365 3.5 31.5 1.0 CZ D:ARG365 3.5 35.7 1.0 C15 D:KMA503 3.6 66.7 1.0 C11 D:KMA503 3.6 61.5 1.0 CH2 D:TRP447 3.8 39.0 1.0 CGA D:HEM502 3.9 64.2 1.0 C12 C:KMA510 4.0 53.2 1.0 O2A D:HEM502 4.0 71.8 1.0 C16 D:KMA503 4.1 65.6 1.0 CE3 D:TRP447 4.2 32.9 1.0 F13 C:KMA510 4.2 53.8 1.0 O D:HOH805 4.2 25.4 1.0 NH1 D:ARG365 4.3 35.0 1.0 CD D:ARG365 4.3 26.6 1.0 C13 C:KMA510 4.5 57.7 1.0 CAA D:HEM502 4.5 32.1 1.0 O D:HOH816 4.7 36.7 1.0 O1A D:HEM502 4.8 78.3 1.0 C17 D:KMA503 4.8 71.5 1.0 CZ2 D:TRP447 4.9 37.3 1.0 C09 D:KMA503 4.9 51.1 1.0 C11 C:KMA510 5.0 55.5 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