Iron in PDB 5fvw: Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine, PDB code: 5fvw 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)	50.080 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.590, 121.910, 164.060, 90.00, 90.00, 90.00
R / Rfree (%)	19.42 / 24.94

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

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine (pdb code 5fvw). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine, PDB code: 5fvw:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-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 Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:28.8 occ:1.00 FE A:HEM750 0.0 28.8 1.0 ND A:HEM750 2.0 27.9 1.0 NC A:HEM750 2.0 21.7 1.0 NA A:HEM750 2.0 36.1 1.0 NB A:HEM750 2.1 28.0 1.0 SG A:CYS420 2.4 27.9 1.0 C1A A:HEM750 3.0 30.0 1.0 C4D A:HEM750 3.0 28.6 1.0 C1C A:HEM750 3.1 22.9 1.0 C1D A:HEM750 3.1 28.3 1.0 C4C A:HEM750 3.1 23.9 1.0 C4B A:HEM750 3.1 29.1 1.0 C1B A:HEM750 3.1 31.6 1.0 C4A A:HEM750 3.1 31.4 1.0 CHA A:HEM750 3.4 24.2 1.0 CB A:CYS420 3.4 27.2 1.0 CHD A:HEM750 3.4 28.4 1.0 CHC A:HEM750 3.4 23.7 1.0 CHB A:HEM750 3.5 31.0 1.0 C03 A:W66800 4.0 32.2 1.0 CA A:CYS420 4.2 26.1 1.0 C04 A:W66800 4.2 33.4 1.0 C2A A:HEM750 4.3 29.5 1.0 C3D A:HEM750 4.3 25.0 1.0 C2D A:HEM750 4.3 16.0 1.0 C07 A:W66800 4.3 32.9 1.0 C3C A:HEM750 4.3 23.4 1.0 C3B A:HEM750 4.3 28.4 1.0 C2C A:HEM750 4.3 24.6 1.0 C3A A:HEM750 4.3 32.3 1.0 C2B A:HEM750 4.3 27.7 1.0 NE1 A:TRP414 4.4 24.5 1.0 C02 A:W66800 4.6 29.7 1.0 N A:GLY422 4.7 25.4 1.0 C A:CYS420 4.8 24.6 1.0 N A:VAL421 4.8 24.6 1.0 C05 A:W66800 4.9 35.6 1.0 N02 A:W66800 5.0 24.9 1.0

Iron binding site 2 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-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 Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(3-(Methylamino)Propyl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:30.1 occ:1.00 FE B:HEM750 0.0 30.1 1.0 ND B:HEM750 2.0 28.9 1.0 NC B:HEM750 2.1 27.5 1.0 NB B:HEM750 2.1 30.4 1.0 NA B:HEM750 2.1 29.2 1.0 SG B:CYS420 2.4 30.4 1.0 C4D B:HEM750 3.0 33.7 1.0 C1C B:HEM750 3.0 34.7 1.0 C4B B:HEM750 3.1 32.3 1.0 C1A B:HEM750 3.1 27.6 1.0 C1D B:HEM750 3.1 29.7 1.0 C4C B:HEM750 3.1 29.3 1.0 C1B B:HEM750 3.1 35.6 1.0 C4A B:HEM750 3.2 32.6 1.0 CHA B:HEM750 3.4 24.6 1.0 CHC B:HEM750 3.4 31.8 1.0 CB B:CYS420 3.4 30.3 1.0 CHD B:HEM750 3.5 34.5 1.0 CHB B:HEM750 3.5 41.0 1.0 C03 B:W66800 3.9 24.4 1.0 C07 B:W66800 4.1 33.0 1.0 C04 B:W66800 4.1 29.1 1.0 CA B:CYS420 4.2 28.1 1.0 C3D B:HEM750 4.3 34.1 1.0 C3B B:HEM750 4.3 28.6 1.0 C2C B:HEM750 4.3 34.0 1.0 C2D B:HEM750 4.3 21.8 1.0 C2B B:HEM750 4.3 29.6 1.0 C3C B:HEM750 4.3 33.6 1.0 C2A B:HEM750 4.3 29.1 1.0 NE1 B:TRP414 4.4 29.9 1.0 C3A B:HEM750 4.4 33.9 1.0 C02 B:W66800 4.7 28.3 1.0 N B:GLY422 4.8 34.5 1.0 C B:CYS420 4.9 23.8 1.0 N B:VAL421 4.9 28.6 1.0 C05 B:W66800 5.0 31.0 1.0

H.Wang, Y.Qin, H.Li, L.J.Roman, P.Martasek, T.L.Poulos, R.B.Silverman. Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibition By Optimization of the 2-Aminopyridine-Based Scaffold with A Pyridine Linker. J.Med.Chem. V. 59 4913 2016.
ISSN: ISSN 0022-2623
PubMed: 27050842
DOI: 10.1021/ACS.JMEDCHEM.6B00273