Iron in PDB 4uch: Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile, PDB code: 4uch 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)	50.025 / 2.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.000, 122.380, 164.440, 90.00, 90.00, 90.00
R / Rfree (%)	19.42 / 25.1

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile 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 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile (pdb code 4uch). 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 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile, PDB code: 4uch:
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 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile


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 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:32.5 occ:1.00 FE A:HEM750 0.0 32.5 1.0 NB A:HEM750 2.0 26.1 1.0 NC A:HEM750 2.0 27.7 1.0 ND A:HEM750 2.0 28.4 1.0 NA A:HEM750 2.1 32.3 1.0 SG A:CYS420 2.3 31.1 1.0 N01 A:OLW800 2.4 41.8 1.0 C1B A:HEM750 3.0 39.0 1.0 C4B A:HEM750 3.0 29.6 1.0 C1D A:HEM750 3.0 34.1 1.0 C1C A:HEM750 3.0 28.7 1.0 C4C A:HEM750 3.1 29.7 1.0 C4D A:HEM750 3.1 33.7 1.0 C4A A:HEM750 3.1 34.5 1.0 C1A A:HEM750 3.1 19.4 1.0 C02 A:OLW800 3.1 41.9 1.0 CB A:CYS420 3.3 37.2 1.0 CHC A:HEM750 3.4 27.4 1.0 CHD A:HEM750 3.4 33.8 1.0 CHB A:HEM750 3.4 33.8 1.0 CHA A:HEM750 3.5 23.7 1.0 C05 A:OLW800 3.5 33.5 1.0 CA A:CYS420 4.1 32.9 1.0 C2B A:HEM750 4.2 33.6 1.0 C3B A:HEM750 4.2 31.6 1.0 C2C A:HEM750 4.3 27.6 1.0 C2D A:HEM750 4.3 26.1 1.0 C3C A:HEM750 4.3 29.5 1.0 C3D A:HEM750 4.3 31.1 1.0 C3A A:HEM750 4.3 30.7 1.0 C2A A:HEM750 4.3 32.7 1.0 N03 A:OLW800 4.3 46.9 1.0 NE1 A:TRP414 4.5 28.5 1.0 C04 A:OLW800 4.6 40.7 1.0 N A:GLY422 4.8 36.8 1.0 C A:CYS420 4.8 31.3 1.0 O A:HOH2145 4.9 29.0 1.0 CE1 A:PHE589 4.9 36.9 1.0 N A:VAL421 4.9 27.9 1.0

Iron binding site 2 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile


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 3-(((2-((2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl) Ethyl)Amino)Methyl)Benzonitrile within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:30.2 occ:1.00 FE B:HEM750 0.0 30.2 1.0 NB B:HEM750 2.0 38.6 1.0 NC B:HEM750 2.1 31.8 1.0 ND B:HEM750 2.1 32.3 1.0 NA B:HEM750 2.1 40.5 1.0 SG B:CYS420 2.3 33.4 1.0 N01 B:OLW800 2.3 32.7 1.0 C4B B:HEM750 3.0 42.6 1.0 C1B B:HEM750 3.0 40.3 1.0 C1C B:HEM750 3.0 36.1 1.0 C4A B:HEM750 3.1 36.8 1.0 C4D B:HEM750 3.1 37.1 1.0 C1D B:HEM750 3.1 33.8 1.0 C4C B:HEM750 3.1 33.5 1.0 C05 B:OLW800 3.1 30.7 1.0 C1A B:HEM750 3.1 33.3 1.0 CB B:CYS420 3.3 30.6 1.0 C02 B:OLW800 3.3 34.8 1.0 CHC B:HEM750 3.4 38.4 1.0 CHB B:HEM750 3.4 38.9 1.0 CHA B:HEM750 3.4 30.4 1.0 CHD B:HEM750 3.4 33.8 1.0 CA B:CYS420 4.2 28.9 1.0 C3B B:HEM750 4.2 41.0 1.0 C2B B:HEM750 4.2 34.3 1.0 C2C B:HEM750 4.3 43.2 1.0 C3A B:HEM750 4.3 37.0 1.0 C2A B:HEM750 4.3 35.4 1.0 C3C B:HEM750 4.3 38.7 1.0 C3D B:HEM750 4.3 33.1 1.0 C04 B:OLW800 4.3 34.5 1.0 N03 B:OLW800 4.3 34.5 1.0 C2D B:HEM750 4.3 28.0 1.0 NE1 B:TRP414 4.5 30.0 1.0 C B:CYS420 4.9 27.3 1.0 N B:GLY422 4.9 33.7 1.0 O B:HOH2110 5.0 45.0 1.0

P.Mukherjee, H.Li, I.F.Sevrioukova, G.Chreifi, P.Martasek, L.J.Roman, T.L.Poulos, R.B.Silverman. Novel 2,4-Disubstituted Pyrimidines As Potent, Selective, and Cell-Permeable Inhibitors of Neuronal Nitric Oxide Synthase. J.Med.Chem. 2014.
ISSN: ESSN 1520-4804
PubMed: 25489882
DOI: 10.1021/JM501719E