Zinc in PDB 6nhf: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-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-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nhf 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)	49.50 / 1.83
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	59.336, 152.557, 108.524, 90.00, 90.70, 90.00
R / Rfree (%)	18.3 / 21.9

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Iron	(Fe)	4 atoms
Gadolinium	(Gd)	4 atoms
Chlorine	(Cl)	4 atoms

The binding sites of Zinc atom in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine (pdb code 6nhf). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine, PDB code: 6nhf:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn507 b:43.8 occ:1.00 SG A:CYS99 2.3 44.5 1.0 SG A:CYS94 2.4 49.7 1.0 SG B:CYS94 2.4 47.2 1.0 SG B:CYS99 2.5 41.6 1.0 CB A:CYS99 3.1 39.9 1.0 CB B:CYS99 3.3 38.4 1.0 CB A:CYS94 3.4 54.7 1.0 CB B:CYS94 3.4 51.2 1.0 CA A:CYS99 3.6 48.2 1.0 CA B:CYS99 3.8 38.8 1.0 N A:GLY101 4.0 50.7 1.0 N A:LEU100 4.1 50.6 1.0 N B:GLY101 4.2 39.4 1.0 C A:CYS99 4.2 56.7 1.0 N B:LEU100 4.3 42.2 1.0 CA A:GLY101 4.3 50.8 1.0 C B:CYS99 4.4 47.9 1.0 CA B:GLY101 4.5 42.7 1.0 CA A:CYS94 4.8 60.4 1.0 CA B:CYS94 4.8 47.3 1.0 N A:CYS99 4.9 44.5 1.0 C A:LEU100 4.9 54.0 1.0

Zinc binding site 2 out of 2 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 2 of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-6-(2,3-Difluoro-5-(2-(1-Methylazetidin-2-Yl)Ethyl) Phenethyl)-4-Methylpyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn507 b:38.2 occ:1.00 SG C:CYS99 2.3 36.6 1.0 SG C:CYS94 2.3 44.2 1.0 SG D:CYS99 2.4 38.3 1.0 SG D:CYS94 2.4 37.2 1.0 CB D:CYS99 3.2 40.0 1.0 CB C:CYS99 3.2 37.6 1.0 CB C:CYS94 3.4 49.4 1.0 CB D:CYS94 3.4 42.6 1.0 CA C:CYS99 3.7 47.6 1.0 CA D:CYS99 3.7 42.7 1.0 N C:GLY101 4.1 38.0 1.0 N D:GLY101 4.1 37.2 1.0 N C:LEU100 4.2 42.3 1.0 N D:LEU100 4.2 36.3 1.0 C C:CYS99 4.3 45.4 1.0 C D:CYS99 4.3 43.1 1.0 CA C:GLY101 4.4 37.8 1.0 CA D:GLY101 4.4 39.0 1.0 CA C:CYS94 4.7 51.5 1.0 CA D:CYS94 4.8 41.5 1.0 C C:LEU100 5.0 45.0 1.0 N D:CYS99 5.0 41.0 1.0 N C:CYS99 5.0 37.0 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