Iron in PDB 6nh3: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-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 (S)-6-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh3 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)	88.87 / 2.01
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.469, 153.089, 109.150, 90.00, 90.80, 90.00
R / Rfree (%)	20.6 / 25.7

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

Fluorine	(F)	8 atoms
Zinc	(Zn)	6 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-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine (pdb code 6nh3). 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-(3-Fluoro-5-(2-(Pyrrolidin-2-Yl)Ethyl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh3:
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-(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 (S)-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:44.1 occ:1.00 FE A:HEM501 0.0 44.1 1.0 ND A:HEM501 2.0 48.7 1.0 NC A:HEM501 2.1 48.1 1.0 NA A:HEM501 2.1 39.9 1.0 NB A:HEM501 2.1 34.3 1.0 SG A:CYS184 2.4 39.5 1.0 C1D A:HEM501 3.0 50.2 1.0 C4C A:HEM501 3.0 50.8 1.0 C4D A:HEM501 3.0 40.1 1.0 C1B A:HEM501 3.1 42.0 1.0 C4A A:HEM501 3.1 41.9 1.0 C1C A:HEM501 3.1 45.3 1.0 C1A A:HEM501 3.1 33.9 1.0 C4B A:HEM501 3.1 40.7 1.0 CHD A:HEM501 3.4 52.8 1.0 CB A:CYS184 3.4 40.3 1.0 CHB A:HEM501 3.4 39.7 1.0 CHA A:HEM501 3.5 39.5 1.0 CHC A:HEM501 3.5 41.8 1.0 C04 A:KL4502 4.0 43.9 1.0 CA A:CYS184 4.1 35.3 1.0 C05 A:KL4502 4.1 48.7 1.0 C2D A:HEM501 4.2 43.6 1.0 C3D A:HEM501 4.2 46.2 1.0 C03 A:KL4502 4.3 38.8 1.0 C3C A:HEM501 4.3 51.9 1.0 C2B A:HEM501 4.3 42.2 1.0 C2C A:HEM501 4.3 53.2 1.0 C07 A:KL4502 4.3 47.1 1.0 C3B A:HEM501 4.3 41.5 1.0 C3A A:HEM501 4.3 39.7 1.0 C2A A:HEM501 4.4 44.4 1.0 NE1 A:TRP178 4.4 41.9 1.0 C06 A:KL4502 4.5 45.8 1.0 C02 A:KL4502 4.6 40.3 1.0 N01 A:KL4502 4.7 46.2 1.0 C A:CYS184 4.8 31.7 1.0 N A:GLY186 4.9 35.3 1.0 N A:VAL185 5.0 31.7 1.0 CD1 A:TRP178 5.0 39.3 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-(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 (S)-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:Fe802 b:27.9 occ:1.00 FE B:HEM802 0.0 27.9 1.0 NA B:HEM802 2.1 27.9 1.0 ND B:HEM802 2.1 32.8 1.0 NB B:HEM802 2.1 29.1 1.0 NC B:HEM802 2.1 24.6 1.0 SG B:CYS184 2.3 26.8 1.0 C1B B:HEM802 3.0 24.9 1.0 C4A B:HEM802 3.0 35.4 1.0 C1D B:HEM802 3.1 33.3 1.0 C4D B:HEM802 3.1 32.9 1.0 C4C B:HEM802 3.1 32.2 1.0 C4B B:HEM802 3.1 29.5 1.0 C1A B:HEM802 3.1 30.4 1.0 C1C B:HEM802 3.1 31.0 1.0 CHB B:HEM802 3.3 23.6 1.0 CHD B:HEM802 3.4 28.8 1.0 CB B:CYS184 3.4 28.4 1.0 CHA B:HEM802 3.5 24.2 1.0 CHC B:HEM802 3.5 26.4 1.0 C04 B:KL4803 4.0 29.4 1.0 CA B:CYS184 4.1 30.6 1.0 C05 B:KL4803 4.2 33.1 1.0 C03 B:KL4803 4.2 28.9 1.0 C2B B:HEM802 4.3 33.0 1.0 C2D B:HEM802 4.3 37.6 1.0 C3B B:HEM802 4.3 27.8 1.0 C3D B:HEM802 4.3 24.8 1.0 C3A B:HEM802 4.3 26.0 1.0 C3C B:HEM802 4.3 35.8 1.0 NE1 B:TRP178 4.3 34.1 1.0 C2A B:HEM802 4.3 28.7 1.0 C2C B:HEM802 4.4 30.7 1.0 C07 B:KL4803 4.5 28.4 1.0 C06 B:KL4803 4.5 37.0 1.0 C02 B:KL4803 4.6 32.2 1.0 N01 B:KL4803 4.7 29.3 1.0 N B:GLY186 4.8 29.9 1.0 C B:CYS184 4.9 26.5 1.0 N B:VAL185 5.0 25.0 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-(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 (S)-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:Fe501 b:39.6 occ:1.00 FE C:HEM501 0.0 39.6 1.0 NC C:HEM501 2.0 47.6 1.0 NA C:HEM501 2.1 44.3 1.0 ND C:HEM501 2.1 45.4 1.0 NB C:HEM501 2.1 38.4 1.0 SG C:CYS184 2.3 38.7 1.0 C4C C:HEM501 3.0 48.8 1.0 C1C C:HEM501 3.0 42.5 1.0 C4A C:HEM501 3.1 43.2 1.0 C1D C:HEM501 3.1 44.3 1.0 C1A C:HEM501 3.1 45.2 1.0 C4B C:HEM501 3.1 36.6 1.0 C1B C:HEM501 3.1 39.2 1.0 C4D C:HEM501 3.1 45.6 1.0 CB C:CYS184 3.2 44.4 1.0 CHD C:HEM501 3.4 47.4 1.0 CHC C:HEM501 3.4 37.8 1.0 CHB C:HEM501 3.5 34.5 1.0 CHA C:HEM501 3.5 43.2 1.0 CA C:CYS184 4.0 37.8 1.0 C04 C:KL4502 4.2 40.8 1.0 C3C C:HEM501 4.2 45.0 1.0 C05 C:KL4502 4.2 45.9 1.0 C2C C:HEM501 4.2 42.8 1.0 C03 C:KL4502 4.3 43.0 1.0 C3A C:HEM501 4.3 37.4 1.0 C2A C:HEM501 4.3 49.5 1.0 C2D C:HEM501 4.3 38.7 1.0 C2B C:HEM501 4.3 40.9 1.0 C3B C:HEM501 4.3 40.6 1.0 NE1 C:TRP178 4.3 38.0 1.0 C3D C:HEM501 4.3 46.5 1.0 C06 C:KL4502 4.5 46.6 1.0 C02 C:KL4502 4.5 44.9 1.0 N01 C:KL4502 4.6 47.1 1.0 C07 C:KL4502 4.6 44.7 1.0 N C:GLY186 4.7 35.8 1.0 C C:CYS184 4.8 31.0 1.0 N C:VAL185 5.0 30.8 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 (S)-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 (S)-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:Fe501 b:25.3 occ:1.00 FE D:HEM501 0.0 25.3 1.0 ND D:HEM501 2.0 27.8 1.0 NC D:HEM501 2.1 23.6 1.0 NA D:HEM501 2.1 26.4 1.0 NB D:HEM501 2.1 21.4 1.0 SG D:CYS184 2.2 25.5 1.0 C1D D:HEM501 3.0 26.6 1.0 C4D D:HEM501 3.1 27.1 1.0 C4A D:HEM501 3.1 25.8 1.0 C1B D:HEM501 3.1 26.8 1.0 C4C D:HEM501 3.1 28.3 1.0 C1C D:HEM501 3.1 25.1 1.0 C1A D:HEM501 3.1 25.6 1.0 C4B D:HEM501 3.2 23.4 1.0 CB D:CYS184 3.3 23.8 1.0 CHD D:HEM501 3.4 23.6 1.0 CHB D:HEM501 3.4 22.6 1.0 CHA D:HEM501 3.5 30.4 1.0 CHC D:HEM501 3.5 21.3 1.0 CA D:CYS184 4.0 21.8 1.0 C04 D:KL4502 4.0 32.1 1.0 C05 D:KL4502 4.2 32.3 1.0 C03 D:KL4502 4.3 29.6 1.0 C3D D:HEM501 4.3 28.6 1.0 C2D D:HEM501 4.3 26.3 1.0 C3A D:HEM501 4.3 27.9 1.0 C2B D:HEM501 4.3 32.0 1.0 C3C D:HEM501 4.3 26.5 1.0 NE1 D:TRP178 4.3 27.6 1.0 C2C D:HEM501 4.3 29.1 1.0 C2A D:HEM501 4.3 27.7 1.0 C3B D:HEM501 4.4 28.8 1.0 C07 D:KL4502 4.4 25.2 1.0 C06 D:KL4502 4.5 35.3 1.0 C02 D:KL4502 4.6 33.9 1.0 N01 D:KL4502 4.7 33.6 1.0 N D:GLY186 4.7 20.8 1.0 C D:CYS184 4.8 24.6 1.0 N D:VAL185 4.9 26.4 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