Iron in PDB 6nh4: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nh4 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)	39.98 / 2.27
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.708, 152.546, 109.139, 90.00, 90.87, 90.00
R / Rfree (%)	19.2 / 25.1

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

Fluorine	(F)	12 atoms
Zinc	(Zn)	6 atoms
Gadolinium	(Gd)	4 atoms
Chlorine	(Cl)	7 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-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine (pdb code 6nh4). 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-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nh4:
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-(2-((2R,4S)-4-Fluoropyrrolidin-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 6-(3-Fluoro-5-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe501 b:28.7 occ:1.00 FE A:HEM501 0.0 28.7 1.0 ND A:HEM501 2.0 31.9 1.0 NC A:HEM501 2.1 37.4 1.0 NA A:HEM501 2.1 23.2 1.0 NB A:HEM501 2.2 33.3 1.0 SG A:CYS184 2.3 22.5 1.0 C4D A:HEM501 3.0 38.1 1.0 C1D A:HEM501 3.0 42.1 1.0 C4C A:HEM501 3.1 33.9 1.0 C1C A:HEM501 3.1 28.3 1.0 C1A A:HEM501 3.1 30.4 1.0 C4B A:HEM501 3.1 35.9 1.0 C1B A:HEM501 3.1 34.0 1.0 C4A A:HEM501 3.2 32.8 1.0 CB A:CYS184 3.3 24.4 1.0 CHD A:HEM501 3.4 36.2 1.0 CHA A:HEM501 3.4 31.7 1.0 CHC A:HEM501 3.5 32.5 1.0 CHB A:HEM501 3.5 35.3 1.0 C04 A:KLA502 4.0 38.1 1.0 CA A:CYS184 4.1 23.2 1.0 C03 A:KLA502 4.2 32.1 1.0 C05 A:KLA502 4.2 42.8 1.0 C3D A:HEM501 4.2 41.4 1.0 C2D A:HEM501 4.2 37.2 1.0 NE1 A:TRP178 4.3 34.6 1.0 C2C A:HEM501 4.3 28.3 1.0 C3C A:HEM501 4.3 33.6 1.0 C2B A:HEM501 4.3 34.7 1.0 C3B A:HEM501 4.3 35.4 1.0 C2A A:HEM501 4.3 37.0 1.0 C3A A:HEM501 4.4 31.9 1.0 C07 A:KLA502 4.4 36.0 1.0 C02 A:KLA502 4.5 31.0 1.0 C06 A:KLA502 4.5 40.9 1.0 N01 A:KLA502 4.7 34.1 1.0 C A:CYS184 4.8 31.2 1.0 N A:GLY186 4.9 31.1 1.0 N A:VAL185 4.9 26.6 1.0 CD1 A:TRP178 4.9 29.7 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-(2-((2R,4S)-4-Fluoropyrrolidin-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 6-(3-Fluoro-5-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe502 b:15.1 occ:1.00 FE B:HEM502 0.0 15.1 1.0 NA B:HEM502 2.0 12.7 1.0 ND B:HEM502 2.0 12.1 1.0 NB B:HEM502 2.0 14.2 1.0 NC B:HEM502 2.1 5.4 1.0 SG B:CYS184 2.4 16.0 1.0 C4A B:HEM502 3.0 18.4 1.0 C1B B:HEM502 3.0 10.0 1.0 C1A B:HEM502 3.0 10.0 1.0 C4D B:HEM502 3.0 13.5 1.0 C4B B:HEM502 3.1 14.1 1.0 C1D B:HEM502 3.1 12.5 1.0 C1C B:HEM502 3.1 12.9 1.0 C4C B:HEM502 3.1 7.0 1.0 CB B:CYS184 3.3 13.4 1.0 CHB B:HEM502 3.4 17.8 1.0 CHA B:HEM502 3.4 11.0 1.0 CHC B:HEM502 3.5 11.7 1.0 CHD B:HEM502 3.5 9.7 1.0 C04 B:KLA503 4.0 19.3 1.0 CA B:CYS184 4.0 13.3 1.0 C05 B:KLA503 4.0 12.2 1.0 C2B B:HEM502 4.2 15.2 1.0 C3A B:HEM502 4.2 9.9 1.0 C2A B:HEM502 4.2 12.7 1.0 C3B B:HEM502 4.3 15.2 1.0 C03 B:KLA503 4.3 3.8 1.0 C3D B:HEM502 4.3 12.8 1.0 C2D B:HEM502 4.3 14.4 1.0 C07 B:KLA503 4.3 10.6 1.0 C06 B:KLA503 4.4 17.0 1.0 C3C B:HEM502 4.4 10.2 1.0 C2C B:HEM502 4.4 9.5 1.0 NE1 B:TRP178 4.4 13.9 1.0 C02 B:KLA503 4.6 10.7 1.0 N01 B:KLA503 4.6 11.7 1.0 N B:GLY186 4.8 17.5 1.0 C B:CYS184 4.8 15.3 1.0 N B:VAL185 5.0 13.4 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-(2-((2R,4S)-4-Fluoropyrrolidin-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 6-(3-Fluoro-5-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe502 b:28.6 occ:1.00 FE C:HEM502 0.0 28.6 1.0 ND C:HEM502 2.0 28.5 1.0 NC C:HEM502 2.1 28.5 1.0 NA C:HEM502 2.1 32.3 1.0 NB C:HEM502 2.2 38.1 1.0 SG C:CYS184 2.3 23.1 1.0 C1D C:HEM502 3.1 31.2 1.0 C4D C:HEM502 3.1 32.7 1.0 C4C C:HEM502 3.1 24.6 1.0 C1B C:HEM502 3.1 39.9 1.0 C4A C:HEM502 3.1 34.9 1.0 C1C C:HEM502 3.1 30.6 1.0 C1A C:HEM502 3.1 31.0 1.0 C4B C:HEM502 3.2 38.3 1.0 CB C:CYS184 3.3 19.0 1.0 CHD C:HEM502 3.4 19.1 1.0 CHA C:HEM502 3.5 23.2 1.0 CHB C:HEM502 3.5 37.6 1.0 CHC C:HEM502 3.5 31.5 1.0 C04 C:KLA504 4.0 29.0 1.0 CA C:CYS184 4.0 18.1 1.0 C05 C:KLA504 4.1 38.6 1.0 C03 C:KLA504 4.2 30.4 1.0 C3D C:HEM502 4.3 32.7 1.0 C2D C:HEM502 4.3 31.9 1.0 C2B C:HEM502 4.3 29.7 1.0 C3B C:HEM502 4.3 31.8 1.0 C3A C:HEM502 4.3 29.4 1.0 C2A C:HEM502 4.3 36.6 1.0 C2C C:HEM502 4.3 29.8 1.0 C3C C:HEM502 4.4 21.4 1.0 C06 C:KLA504 4.4 38.9 1.0 NE1 C:TRP178 4.4 28.3 1.0 C07 C:KLA504 4.5 22.8 1.0 C02 C:KLA504 4.5 32.4 1.0 N01 C:KLA504 4.5 34.2 1.0 N C:GLY186 4.8 24.0 1.0 C C:CYS184 4.8 18.1 1.0 CD1 C:TRP178 5.0 30.0 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-(2-((2R,4S)-4-Fluoropyrrolidin-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 6-(3-Fluoro-5-(2-((2R,4S)-4-Fluoropyrrolidin-2-Yl) Ethyl)Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe501 b:12.3 occ:1.00 FE D:HEM501 0.0 12.3 1.0 ND D:HEM501 2.0 9.5 1.0 NA D:HEM501 2.1 11.8 1.0 NC D:HEM501 2.1 4.5 1.0 NB D:HEM501 2.1 9.2 1.0 SG D:CYS184 2.4 12.3 1.0 C4D D:HEM501 3.0 10.8 1.0 C1D D:HEM501 3.0 19.2 1.0 C1A D:HEM501 3.1 12.6 1.0 C4A D:HEM501 3.1 18.6 1.0 C1B D:HEM501 3.1 9.9 1.0 C4C D:HEM501 3.1 11.5 1.0 C1C D:HEM501 3.1 7.5 1.0 C4B D:HEM501 3.1 7.1 1.0 CB D:CYS184 3.4 11.5 1.0 CHA D:HEM501 3.4 6.6 1.0 CHD D:HEM501 3.4 18.6 1.0 CHB D:HEM501 3.4 9.8 1.0 CHC D:HEM501 3.5 17.1 1.0 C04 D:KLA502 4.0 11.7 1.0 C05 D:KLA502 4.0 2.9 1.0 CA D:CYS184 4.0 11.5 1.0 C3D D:HEM501 4.2 15.3 1.0 C2D D:HEM501 4.2 12.4 1.0 C03 D:KLA502 4.2 5.5 1.0 C2A D:HEM501 4.3 18.9 1.0 C3A D:HEM501 4.3 11.4 1.0 C2B D:HEM501 4.3 9.4 1.0 C3B D:HEM501 4.3 13.2 1.0 C2C D:HEM501 4.3 8.4 1.0 C3C D:HEM501 4.3 3.5 1.0 C07 D:KLA502 4.4 2.7 1.0 NE1 D:TRP178 4.4 13.1 1.0 C06 D:KLA502 4.4 12.6 1.0 C02 D:KLA502 4.6 15.3 1.0 N01 D:KLA502 4.7 9.5 1.0 C D:CYS184 4.8 14.5 1.0 N D:GLY186 4.9 11.9 1.0 N D:VAL185 5.0 15.1 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