Iron 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:

Fluorine	(F)	4 atoms
Zinc	(Zn)	4 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 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 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 6-(3-Fluoro-5-(3-(Methylamino)Prop-1-Yn-1-Yl)Phenethyl)- 4-Methylpyridin-2-Amine, PDB code: 6nh1:
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 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 Iron with other atoms in the Fe 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:Fe501 b:63.6 occ:1.00 FE A:HEM501 0.0 63.6 1.0 NA A:HEM501 2.0 66.6 1.0 ND A:HEM501 2.1 67.3 1.0 NB A:HEM501 2.1 72.3 1.0 NC A:HEM501 2.1 81.0 1.0 SG A:CYS184 2.3 57.8 1.0 C4A A:HEM501 3.0 71.2 1.0 C1B A:HEM501 3.0 74.3 1.0 C4D A:HEM501 3.1 71.6 1.0 C1A A:HEM501 3.1 66.6 1.0 C1D A:HEM501 3.1 82.6 1.0 C4C A:HEM501 3.1 80.2 1.0 C4B A:HEM501 3.1 70.8 1.0 C1C A:HEM501 3.2 81.5 1.0 CB A:CYS184 3.3 60.8 1.0 CHB A:HEM501 3.4 76.2 1.0 CHA A:HEM501 3.4 74.3 1.0 CHD A:HEM501 3.4 88.0 1.0 CHC A:HEM501 3.5 76.2 1.0 C04 A:KLY502 3.9 67.0 1.0 CA A:CYS184 4.0 59.6 1.0 C05 A:KLY502 4.1 72.4 1.0 C03 A:KLY502 4.1 58.0 1.0 C07 A:KLY502 4.2 65.0 1.0 C2B A:HEM501 4.2 66.0 1.0 C3A A:HEM501 4.3 71.4 1.0 C3B A:HEM501 4.3 62.2 1.0 C2A A:HEM501 4.3 77.1 1.0 C3D A:HEM501 4.3 71.8 1.0 C2D A:HEM501 4.3 74.6 1.0 C3C A:HEM501 4.4 81.7 1.0 C2C A:HEM501 4.4 82.7 1.0 C06 A:KLY502 4.5 69.6 1.0 C02 A:KLY502 4.6 62.9 1.0 NE1 A:TRP178 4.7 58.0 1.0 N01 A:KLY502 4.8 59.7 1.0 N A:VAL185 4.8 57.0 1.0 C A:CYS184 4.8 61.8 1.0 N A:GLY186 4.9 70.1 1.0

Iron 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 Iron with other atoms in the Fe 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:Fe502 b:49.0 occ:1.00 FE B:HEM502 0.0 49.0 1.0 NB B:HEM502 2.1 61.0 1.0 ND B:HEM502 2.1 53.0 1.0 NC B:HEM502 2.1 71.8 1.0 NA B:HEM502 2.1 64.9 1.0 SG B:CYS184 2.2 37.0 1.0 C1B B:HEM502 3.0 61.6 1.0 C4A B:HEM502 3.1 64.8 1.0 C1D B:HEM502 3.1 54.4 1.0 C4C B:HEM502 3.1 68.5 1.0 C4D B:HEM502 3.1 66.6 1.0 C4B B:HEM502 3.1 66.5 1.0 C1C B:HEM502 3.1 70.5 1.0 C1A B:HEM502 3.2 62.9 1.0 CB B:CYS184 3.3 39.2 1.0 CHB B:HEM502 3.4 57.3 1.0 CHD B:HEM502 3.4 48.4 1.0 CHC B:HEM502 3.5 70.5 1.0 CHA B:HEM502 3.5 56.1 1.0 CA B:CYS184 4.0 52.7 1.0 C04 B:KLY504 4.1 66.4 1.0 C03 B:KLY504 4.2 62.1 1.0 C2B B:HEM502 4.2 67.6 1.0 C05 B:KLY504 4.3 67.6 1.0 C2D B:HEM502 4.3 60.1 1.0 C3D B:HEM502 4.3 63.0 1.0 C3B B:HEM502 4.3 65.7 1.0 C3C B:HEM502 4.3 71.6 1.0 C3A B:HEM502 4.3 67.6 1.0 C2C B:HEM502 4.3 72.5 1.0 NE1 B:TRP178 4.4 48.0 1.0 C2A B:HEM502 4.4 63.9 1.0 C02 B:KLY504 4.4 56.5 1.0 C06 B:KLY504 4.5 62.1 1.0 C07 B:KLY504 4.6 62.6 1.0 N01 B:KLY504 4.6 57.9 1.0 N B:GLY186 4.8 48.6 1.0 C B:CYS184 4.8 49.8 1.0 N B:VAL185 5.0 41.7 1.0

Iron 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 Iron with other atoms in the Fe 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:Fe501 b:59.3 occ:1.00 FE C:HEM501 0.0 59.3 1.0 NC C:HEM501 2.0 82.4 1.0 ND C:HEM501 2.1 72.4 1.0 NA C:HEM501 2.1 74.5 1.0 NB C:HEM501 2.2 74.2 1.0 SG C:CYS184 2.3 49.7 1.0 C1C C:HEM501 3.0 83.2 1.0 C4C C:HEM501 3.1 85.7 1.0 C1A C:HEM501 3.1 62.3 1.0 C4D C:HEM501 3.1 67.4 1.0 C1D C:HEM501 3.1 79.2 1.0 C4A C:HEM501 3.1 74.4 1.0 C4B C:HEM501 3.1 63.9 1.0 C1B C:HEM501 3.2 78.0 1.0 CB C:CYS184 3.2 52.2 1.0 CHA C:HEM501 3.4 58.5 1.0 CHC C:HEM501 3.4 66.0 1.0 CHD C:HEM501 3.4 80.7 1.0 CHB C:HEM501 3.6 66.1 1.0 CA C:CYS184 4.0 48.4 1.0 C04 C:KLY503 4.0 74.2 1.0 C03 C:KLY503 4.2 76.4 1.0 C05 C:KLY503 4.2 78.8 1.0 C2C C:HEM501 4.3 86.5 1.0 C3C C:HEM501 4.3 83.9 1.0 C2A C:HEM501 4.3 73.2 1.0 C3D C:HEM501 4.3 68.0 1.0 C2D C:HEM501 4.3 69.8 1.0 C3A C:HEM501 4.3 64.3 1.0 C3B C:HEM501 4.4 70.6 1.0 C2B C:HEM501 4.4 71.0 1.0 C06 C:KLY503 4.4 71.1 1.0 C02 C:KLY503 4.4 71.5 1.0 NE1 C:TRP178 4.5 69.5 1.0 C07 C:KLY503 4.5 68.2 1.0 N01 C:KLY503 4.5 69.0 1.0 N C:GLY186 4.7 65.0 1.0 C C:CYS184 4.8 51.7 1.0 N C:VAL185 5.0 58.2 1.0

Iron 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 Iron with other atoms in the Fe 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:Fe501 b:43.9 occ:1.00 FE D:HEM501 0.0 43.9 1.0 ND D:HEM501 2.1 60.2 1.0 NA D:HEM501 2.1 63.9 1.0 NC D:HEM501 2.1 59.0 1.0 SG D:CYS184 2.1 34.7 1.0 NB D:HEM501 2.2 56.2 1.0 C4A D:HEM501 3.0 57.9 1.0 C1D D:HEM501 3.0 62.0 1.0 C1B D:HEM501 3.1 57.7 1.0 C4C D:HEM501 3.1 60.8 1.0 C4D D:HEM501 3.1 67.9 1.0 CB D:CYS184 3.1 34.9 1.0 C1A D:HEM501 3.2 64.8 1.0 C1C D:HEM501 3.2 68.0 1.0 C4B D:HEM501 3.2 62.9 1.0 CHB D:HEM501 3.4 42.7 1.0 CHD D:HEM501 3.4 50.2 1.0 CHA D:HEM501 3.5 67.9 1.0 CHC D:HEM501 3.6 64.5 1.0 C03 D:KLY503 3.9 73.9 1.0 C04 D:KLY503 3.9 81.2 1.0 CA D:CYS184 4.0 38.0 1.0 C07 D:KLY503 4.2 79.6 1.0 C3A D:HEM501 4.3 67.6 1.0 C2D D:HEM501 4.3 61.0 1.0 NE1 D:TRP178 4.3 60.4 1.0 C3D D:HEM501 4.3 59.6 1.0 C2A D:HEM501 4.3 62.3 1.0 C2B D:HEM501 4.3 63.2 1.0 C3C D:HEM501 4.3 64.0 1.0 C02 D:KLY503 4.4 70.0 1.0 C2C D:HEM501 4.4 63.4 1.0 C3B D:HEM501 4.4 63.8 1.0 C05 D:KLY503 4.4 73.0 1.0 C D:CYS184 4.8 37.5 1.0 N01 D:KLY503 4.8 71.1 1.0 N D:VAL185 4.8 52.1 1.0 C06 D:KLY503 4.9 67.4 1.0 N02 D:KLY503 4.9 70.3 1.0 CD1 D:TRP178 5.0 60.5 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