Iron 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:

Fluorine	(F)	6 atoms
Zinc	(Zn)	6 atoms
Gadolinium	(Gd)	2 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 (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 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 (R)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh2:
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 (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 Iron with other atoms in the Fe 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:Fe501 b:28.1 occ:1.00 FE A:HEM501 0.0 28.1 1.0 NA A:HEM501 2.0 30.9 1.0 ND A:HEM501 2.1 34.0 1.0 NC A:HEM501 2.1 34.7 1.0 NB A:HEM501 2.1 32.3 1.0 SG A:CYS184 2.3 23.6 1.0 C4A A:HEM501 3.0 33.4 1.0 C1B A:HEM501 3.0 23.0 1.0 C1D A:HEM501 3.1 34.6 1.0 C1A A:HEM501 3.1 30.6 1.0 C4D A:HEM501 3.1 31.6 1.0 C4C A:HEM501 3.1 34.4 1.0 C1C A:HEM501 3.1 33.5 1.0 C4B A:HEM501 3.1 28.9 1.0 CHB A:HEM501 3.4 22.9 1.0 CB A:CYS184 3.4 22.8 1.0 CHD A:HEM501 3.4 27.6 1.0 CHA A:HEM501 3.4 32.5 1.0 CHC A:HEM501 3.5 27.7 1.0 C04 A:KMA503 3.9 41.9 1.0 C05 A:KMA503 4.0 44.6 1.0 CA A:CYS184 4.1 20.7 1.0 C03 A:KMA503 4.2 31.4 1.0 C3A A:HEM501 4.3 34.5 1.0 C2B A:HEM501 4.3 27.4 1.0 C2A A:HEM501 4.3 33.4 1.0 C07 A:KMA503 4.3 50.8 1.0 C3D A:HEM501 4.3 36.8 1.0 C2D A:HEM501 4.3 33.9 1.0 C3B A:HEM501 4.3 31.1 1.0 C3C A:HEM501 4.3 27.4 1.0 C2C A:HEM501 4.3 33.2 1.0 C06 A:KMA503 4.4 45.5 1.0 NE1 A:TRP178 4.4 30.8 1.0 C02 A:KMA503 4.5 36.6 1.0 N01 A:KMA503 4.6 43.0 1.0 N A:GLY186 4.9 29.9 1.0 C A:CYS184 4.9 21.5 1.0 N A:VAL185 5.0 28.3 1.0

Iron binding site 2 out of 4 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 Iron with other atoms in the Fe 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 B:Fe501 b:18.5 occ:1.00 FE B:HEM501 0.0 18.5 1.0 ND B:HEM501 2.0 16.9 1.0 NA B:HEM501 2.1 15.7 1.0 NC B:HEM501 2.1 16.3 1.0 NB B:HEM501 2.1 22.9 1.0 SG B:CYS184 2.4 14.5 1.0 C1D B:HEM501 3.0 17.7 1.0 C4D B:HEM501 3.1 20.7 1.0 C1B B:HEM501 3.1 18.0 1.0 C4A B:HEM501 3.1 16.1 1.0 C4C B:HEM501 3.1 20.9 1.0 C1A B:HEM501 3.1 16.1 1.0 C1C B:HEM501 3.1 21.9 1.0 C4B B:HEM501 3.1 14.6 1.0 CHB B:HEM501 3.4 16.3 1.0 CB B:CYS184 3.4 14.7 1.0 CHD B:HEM501 3.4 18.4 1.0 CHA B:HEM501 3.4 14.0 1.0 CHC B:HEM501 3.5 20.2 1.0 C04 B:KMA502 4.0 53.4 1.0 CA B:CYS184 4.0 16.5 1.0 C05 B:KMA502 4.1 55.0 1.0 C3D B:HEM501 4.3 16.2 1.0 C2D B:HEM501 4.3 16.9 1.0 C03 B:KMA502 4.3 53.5 1.0 C2B B:HEM501 4.3 19.6 1.0 C07 B:KMA502 4.3 50.9 1.0 C3A B:HEM501 4.3 15.9 1.0 C3B B:HEM501 4.3 14.1 1.0 C3C B:HEM501 4.3 22.7 1.0 C2C B:HEM501 4.3 22.5 1.0 C2A B:HEM501 4.3 17.1 1.0 NE1 B:TRP178 4.3 20.0 1.0 C06 B:KMA502 4.5 49.8 1.0 C02 B:KMA502 4.6 42.4 1.0 N01 B:KMA502 4.8 41.5 1.0 N B:GLY186 4.8 19.2 1.0 C B:CYS184 4.9 18.7 1.0 N B:VAL185 5.0 16.1 1.0

Iron binding site 3 out of 4 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 Iron with other atoms in the Fe 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 C:Fe502 b:24.1 occ:1.00 FE C:HEM502 0.0 24.1 1.0 ND C:HEM502 2.0 21.9 1.0 NC C:HEM502 2.0 29.9 1.0 NA C:HEM502 2.1 32.4 1.0 NB C:HEM502 2.1 24.2 1.0 SG C:CYS184 2.4 22.9 1.0 C1D C:HEM502 3.0 30.4 1.0 C4D C:HEM502 3.0 30.1 1.0 C4C C:HEM502 3.1 28.6 1.0 C4A C:HEM502 3.1 33.3 1.0 C1C C:HEM502 3.1 33.6 1.0 C1B C:HEM502 3.1 34.1 1.0 C1A C:HEM502 3.1 30.1 1.0 C4B C:HEM502 3.1 25.2 1.0 CB C:CYS184 3.3 18.5 1.0 CHD C:HEM502 3.4 26.3 1.0 CHA C:HEM502 3.4 22.9 1.0 CHB C:HEM502 3.5 37.8 1.0 CHC C:HEM502 3.5 23.4 1.0 CA C:CYS184 4.0 21.8 1.0 C04 C:KMA504 4.0 41.3 1.0 C05 C:KMA504 4.1 37.4 1.0 C3D C:HEM502 4.2 33.5 1.0 C2D C:HEM502 4.2 25.6 1.0 C3C C:HEM502 4.3 32.3 1.0 C3A C:HEM502 4.3 33.0 1.0 C2C C:HEM502 4.3 35.7 1.0 C03 C:KMA504 4.3 32.6 1.0 C2B C:HEM502 4.3 32.5 1.0 NE1 C:TRP178 4.3 24.9 1.0 C3B C:HEM502 4.3 30.6 1.0 C2A C:HEM502 4.3 36.3 1.0 C06 C:KMA504 4.4 42.2 1.0 C07 C:KMA504 4.5 50.8 1.0 C02 C:KMA504 4.6 31.8 1.0 N01 C:KMA504 4.7 33.4 1.0 N C:GLY186 4.8 22.6 1.0 C C:CYS184 4.8 24.1 1.0 N C:VAL185 4.9 21.8 1.0 CD1 C:TRP178 5.0 35.2 1.0

Iron binding site 4 out of 4 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 Iron with other atoms in the Fe 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 D:Fe502 b:17.4 occ:1.00 FE D:HEM502 0.0 17.4 1.0 NA D:HEM502 2.0 15.9 1.0 ND D:HEM502 2.1 16.5 1.0 NB D:HEM502 2.1 19.1 1.0 NC D:HEM502 2.2 15.4 1.0 SG D:CYS184 2.4 12.3 1.0 C4A D:HEM502 3.0 22.6 1.0 C1B D:HEM502 3.0 20.2 1.0 C1A D:HEM502 3.1 20.4 1.0 C4D D:HEM502 3.1 18.5 1.0 C1D D:HEM502 3.1 18.4 1.0 C4B D:HEM502 3.1 17.3 1.0 C4C D:HEM502 3.1 19.9 1.0 C1C D:HEM502 3.2 18.3 1.0 CHB D:HEM502 3.3 14.5 1.0 CB D:CYS184 3.4 15.5 1.0 CHA D:HEM502 3.4 11.7 1.0 CHD D:HEM502 3.5 20.9 1.0 CHC D:HEM502 3.5 19.1 1.0 C04 D:KMA503 4.0 53.4 1.0 CA D:CYS184 4.1 12.5 1.0 C05 D:KMA503 4.1 55.0 1.0 C03 D:KMA503 4.2 53.5 1.0 C2B D:HEM502 4.2 18.1 1.0 C3A D:HEM502 4.2 14.0 1.0 C2A D:HEM502 4.3 16.9 1.0 C3B D:HEM502 4.3 22.0 1.0 C3D D:HEM502 4.3 16.3 1.0 C2D D:HEM502 4.3 15.8 1.0 C3C D:HEM502 4.4 17.5 1.0 C2C D:HEM502 4.4 15.5 1.0 NE1 D:TRP178 4.4 16.4 1.0 C07 D:KMA503 4.4 50.9 1.0 C06 D:KMA503 4.5 49.8 1.0 C02 D:KMA503 4.5 42.4 1.0 N01 D:KMA503 4.6 41.5 1.0 N D:GLY186 4.8 17.2 1.0 C D:CYS184 4.9 13.4 1.0 N D:VAL185 4.9 20.6 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