Zinc in PDB 4v3u: Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine, PDB code: 4v3u 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)	78.798 / 2.30
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	175.559, 84.630, 167.269, 90.00, 91.96, 90.00
R / Rfree (%)	18.89 / 23.49

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine also contains other interesting chemical elements:

Iron

(Fe)

4 atoms

The binding sites of Zinc atom in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine (pdb code 4v3u). 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 Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine, PDB code: 4v3u:
Jump to Zinc binding site number: 1; 2;

Zinc binding site 1 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-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 Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine within 5.0Å range: probe atom residue distance (Å) B Occ A:Zn900 b:21.8 occ:1.00 SG B:CYS336 2.3 23.2 1.0 SG A:CYS331 2.3 16.9 1.0 SG B:CYS331 2.4 16.4 1.0 SG A:CYS336 2.4 19.1 1.0 CB B:CYS336 3.1 20.4 1.0 CB A:CYS336 3.3 17.2 1.0 CB B:CYS331 3.4 16.9 1.0 CA B:CYS336 3.5 17.2 1.0 CB A:CYS331 3.5 25.9 1.0 CA A:CYS336 3.6 17.3 1.0 N A:MET337 3.8 19.9 1.0 N B:MET337 3.8 24.6 1.0 C B:CYS336 4.0 28.6 1.0 N B:GLY338 4.1 18.9 1.0 C A:CYS336 4.2 22.2 1.0 N A:GLY338 4.2 17.1 1.0 CA B:GLY338 4.6 20.3 1.0 CA A:GLY338 4.7 26.0 1.0 N B:CYS336 4.8 25.4 1.0 CA B:CYS331 4.8 25.6 1.0 CA A:CYS331 4.8 23.6 1.0 C A:MET337 4.9 21.9 1.0 CA A:MET337 4.9 20.3 1.0 N A:CYS336 4.9 17.6 1.0 C B:MET337 4.9 19.0 1.0 O B:ILE335 4.9 23.4 1.0 CA B:MET337 5.0 16.9 1.0

Zinc binding site 2 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-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 Nnos R354A G357D Mutant Heme Domain in Complex with N-2-(2-(1H-Imidazol-1-Yl)Pyrimidin-4-Yl)Ethyl- 3-(Pyridin-3-Yl)Propan-1-Amine within 5.0Å range: probe atom residue distance (Å) B Occ C:Zn900 b:23.2 occ:1.00 SG C:CYS331 2.3 20.2 1.0 SG D:CYS331 2.3 18.9 1.0 SG D:CYS336 2.4 21.9 1.0 SG C:CYS336 2.4 15.8 1.0 CB D:CYS336 3.2 21.2 1.0 CB C:CYS336 3.3 16.4 1.0 CB C:CYS331 3.4 23.2 1.0 CB D:CYS331 3.4 16.6 1.0 CA D:CYS336 3.6 16.1 1.0 CA C:CYS336 3.6 19.8 1.0 N C:MET337 3.8 23.5 1.0 N D:MET337 3.9 16.7 1.0 N C:GLY338 4.0 15.3 1.0 C C:CYS336 4.1 24.4 1.0 C D:CYS336 4.1 16.1 1.0 N D:GLY338 4.2 15.6 1.0 CA C:GLY338 4.5 24.6 1.0 CA D:GLY338 4.7 15.4 1.0 CA C:CYS331 4.7 28.7 1.0 CA D:CYS331 4.8 21.1 1.0 O C:HOH2017 4.8 31.7 1.0 C C:MET337 4.8 29.3 1.0 N D:CYS336 4.9 23.4 1.0 N C:CYS336 4.9 25.4 1.0 CA C:MET337 4.9 21.8 1.0 O D:ILE335 5.0 24.9 1.0 C D:MET337 5.0 18.1 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