Zinc in PDB 4uh6: Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile, PDB code: 4uh6 was solved by H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	39.789 / 1.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.270, 122.710, 164.960, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 21.3

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile also contains other interesting chemical elements:

Iron	(Fe)	2 atoms
Chlorine	(Cl)	2 atoms

The binding sites of Zinc atom in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile (pdb code 4uh6). This binding sites where shown within 5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile, PDB code: 4uh6:

Zinc binding site 1 out of 1 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile


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 Nnos R354A G357D Mutant Heme Domain in Complex with 3-(2-(6-Amino-4-Methylpyridin-2-Yl)Ethyl)-5-( Methyl(2-(Methylamino)Ethyl)Amino)Benzonitrile within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:33.5 occ:1.00 SG B:CYS336 2.3 33.2 1.0 SG A:CYS336 2.3 33.0 1.0 SG A:CYS331 2.3 35.6 1.0 SG B:CYS331 2.4 34.1 1.0 CB A:CYS336 3.1 33.6 1.0 CB B:CYS336 3.2 37.1 1.0 CB A:CYS331 3.3 37.2 1.0 CB B:CYS331 3.4 33.4 1.0 CA B:CYS336 3.6 37.2 1.0 CA A:CYS336 3.6 37.0 1.0 N A:MET337 4.0 37.8 1.0 N B:MET337 4.0 35.7 1.0 C B:CYS336 4.2 38.3 1.0 N B:GLY338 4.2 36.4 1.0 C A:CYS336 4.2 36.5 1.0 N A:GLY338 4.3 28.6 1.0 O B:HOH2011 4.6 50.8 1.0 CA B:GLY338 4.6 25.8 1.0 CA A:CYS331 4.7 40.5 1.0 CA A:GLY338 4.7 27.5 1.0 CA B:CYS331 4.8 38.9 1.0 O A:HOH2014 4.8 51.6 1.0 N B:CYS336 4.8 34.5 1.0 N A:CYS336 4.9 35.3 1.0

S.Kang, H.Li, W.Tang, P.Martasek, L.J.Roman, T.L.Poulos, R.B.Silverman. 2-Aminopyridines with A Truncated Side Chain to Improve Human Neuronal Nitric Oxide Synthase Inhibitory Potency and Selectivity. J.Med.Chem. V. 58 5548 2015.
ISSN: ISSN 0022-2623
PubMed: 26120733
DOI: 10.1021/ACS.JMEDCHEM.5B00573