Iron in PDB 8ufq: Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride

The structure of Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride, PDB code: 8ufq 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)	38.68 / 1.98
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	117.036, 51.554, 162.279, 90, 90, 90
R / Rfree (%)	18.1 / 22.8

The structure of Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride (pdb code 8ufq). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride, PDB code: 8ufq:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


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 Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:29.6 occ:1.00 FE A:HEM801 0.0 29.6 1.0 ND A:HEM801 2.0 27.2 1.0 NA A:HEM801 2.0 30.1 1.0 NB A:HEM801 2.1 27.1 1.0 NC A:HEM801 2.1 27.4 1.0 SG A:CYS420 2.3 29.7 1.0 O1 A:GOL802 2.6 56.4 1.0 C4D A:HEM801 3.0 31.3 1.0 C1A A:HEM801 3.0 22.1 1.0 C1D A:HEM801 3.1 34.2 1.0 C1B A:HEM801 3.1 31.9 1.0 C4A A:HEM801 3.1 29.4 1.0 C4B A:HEM801 3.1 27.7 1.0 C4C A:HEM801 3.1 28.9 1.0 C1C A:HEM801 3.1 28.8 1.0 CB A:CYS420 3.3 28.5 1.0 CHA A:HEM801 3.4 29.5 1.0 CHB A:HEM801 3.4 27.6 1.0 CHD A:HEM801 3.5 30.6 1.0 CHC A:HEM801 3.5 27.8 1.0 C1 A:GOL802 3.7 52.2 1.0 CA A:CYS420 4.1 25.4 1.0 C3D A:HEM801 4.2 31.5 1.0 C2D A:HEM801 4.2 25.5 1.0 C2B A:HEM801 4.3 31.1 1.0 C2A A:HEM801 4.3 31.3 1.0 C3A A:HEM801 4.3 28.4 1.0 C3B A:HEM801 4.3 28.1 1.0 NE1 A:TRP414 4.3 31.2 1.0 C3C A:HEM801 4.4 23.9 1.0 C2C A:HEM801 4.4 28.3 1.0 C3 A:GOL802 4.7 41.7 1.0 C2 A:GOL802 4.8 48.8 1.0 N A:GLY422 4.8 27.7 1.0 C A:CYS420 4.8 24.4 1.0 N A:VAL421 4.9 27.9 1.0 CD1 A:TRP414 5.0 24.4 1.0

Iron binding site 2 out of 4 in the Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


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 Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe802 b:29.0 occ:1.00 FE B:HEM802 0.0 29.0 1.0 ND B:HEM802 2.0 28.9 1.0 NB B:HEM802 2.0 26.6 1.0 NA B:HEM802 2.1 36.3 1.0 NC B:HEM802 2.1 23.2 1.0 SG B:CYS420 2.3 27.7 1.0 O1 B:GOL803 2.5 67.2 1.0 C4D B:HEM802 3.0 37.2 1.0 C1D B:HEM802 3.0 34.3 1.0 C1B B:HEM802 3.1 30.4 1.0 C4B B:HEM802 3.1 28.1 1.0 C4A B:HEM802 3.1 31.1 1.0 C1A B:HEM802 3.1 33.1 1.0 C4C B:HEM802 3.1 27.4 1.0 C1C B:HEM802 3.1 20.7 1.0 CB B:CYS420 3.3 24.1 1.0 C1 B:GOL803 3.4 65.8 1.0 CHA B:HEM802 3.4 30.0 1.0 CHB B:HEM802 3.4 31.6 1.0 CHD B:HEM802 3.4 22.8 1.0 CHC B:HEM802 3.5 24.0 1.0 CA B:CYS420 4.0 23.2 1.0 C3D B:HEM802 4.2 33.3 1.0 C2D B:HEM802 4.2 29.2 1.0 C2B B:HEM802 4.3 27.2 1.0 C3B B:HEM802 4.3 28.8 1.0 NE1 B:TRP414 4.3 24.3 1.0 C3A B:HEM802 4.3 38.8 1.0 C2A B:HEM802 4.3 38.2 1.0 C3C B:HEM802 4.4 26.2 1.0 C2C B:HEM802 4.4 27.5 1.0 C2 B:GOL803 4.6 56.8 1.0 C B:CYS420 4.7 22.8 1.0 C3 B:GOL803 4.7 47.3 1.0 N B:GLY422 4.7 31.7 1.0 N B:VAL421 4.9 28.4 1.0 CD1 B:TRP414 5.0 26.1 1.0

Iron binding site 3 out of 4 in the Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe801 b:29.6 occ:1.00 FE C:HEM801 0.0 29.6 1.0 ND C:HEM801 2.0 27.4 1.0 NB C:HEM801 2.1 26.1 1.0 NA C:HEM801 2.1 30.8 1.0 NC C:HEM801 2.1 28.8 1.0 SG C:CYS420 2.3 28.7 1.0 O1 C:GOL803 2.4 60.0 1.0 C4D C:HEM801 3.0 33.4 1.0 C1D C:HEM801 3.0 30.5 1.0 C1A C:HEM801 3.1 31.6 1.0 C4C C:HEM801 3.1 23.9 1.0 C1B C:HEM801 3.1 30.9 1.0 C4B C:HEM801 3.1 29.9 1.0 C4A C:HEM801 3.1 32.9 1.0 C1C C:HEM801 3.1 20.9 1.0 CB C:CYS420 3.2 30.3 1.0 CHA C:HEM801 3.4 24.6 1.0 CHD C:HEM801 3.4 25.5 1.0 CHC C:HEM801 3.5 26.9 1.0 CHB C:HEM801 3.5 36.6 1.0 C1 C:GOL803 3.8 60.0 1.0 CA C:CYS420 4.0 23.3 1.0 C3D C:HEM801 4.2 29.9 1.0 C2D C:HEM801 4.2 28.7 1.0 C2B C:HEM801 4.3 26.1 1.0 C3C C:HEM801 4.3 26.7 1.0 C2A C:HEM801 4.3 38.5 1.0 C3B C:HEM801 4.3 28.0 1.0 NE1 C:TRP414 4.3 26.0 1.0 C3A C:HEM801 4.3 36.9 1.0 C3 C:GOL803 4.3 45.2 1.0 C2C C:HEM801 4.3 23.3 1.0 C2 C:GOL803 4.7 47.4 1.0 C C:CYS420 4.7 20.3 1.0 N C:GLY422 4.8 29.5 1.0 N C:VAL421 4.9 24.9 1.0 CD1 C:TRP414 5.0 26.6 1.0

Iron binding site 4 out of 4 in the Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Structure of Human Neuronal Nitric Oxide Synthase R354A/G357D/E597Q Mutant Heme Domain Obtained After Soaking Crystal with 4-Methyl-7-(4- Methyl-2,3,4,5-Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe801 b:29.4 occ:1.00 FE D:HEM801 0.0 29.4 1.0 NB D:HEM801 2.0 26.3 1.0 ND D:HEM801 2.0 26.0 1.0 NA D:HEM801 2.1 31.6 1.0 NC D:HEM801 2.1 26.0 1.0 SG D:CYS420 2.3 27.0 1.0 O1 D:GOL802 2.4 47.8 1.0 C1B D:HEM801 3.0 32.2 1.0 C4B D:HEM801 3.0 29.4 1.0 C4D D:HEM801 3.1 32.1 1.0 C1D D:HEM801 3.1 35.1 1.0 C4A D:HEM801 3.1 26.6 1.0 C1A D:HEM801 3.1 30.0 1.0 C1C D:HEM801 3.1 24.5 1.0 C4C D:HEM801 3.1 28.2 1.0 CB D:CYS420 3.3 26.7 1.0 CHB D:HEM801 3.4 30.5 1.0 CHC D:HEM801 3.4 27.6 1.0 CHA D:HEM801 3.4 30.9 1.0 CHD D:HEM801 3.5 32.8 1.0 C1 D:GOL802 3.8 43.8 1.0 CA D:CYS420 4.0 23.6 1.0 C2B D:HEM801 4.2 31.6 1.0 C3B D:HEM801 4.2 24.9 1.0 C2D D:HEM801 4.3 27.7 1.0 C3D D:HEM801 4.3 29.7 1.0 C3A D:HEM801 4.3 26.9 1.0 NE1 D:TRP414 4.3 30.6 1.0 C2A D:HEM801 4.3 33.5 1.0 C3C D:HEM801 4.4 20.2 1.0 C2C D:HEM801 4.4 25.9 1.0 C3 D:GOL802 4.5 40.5 1.0 N D:GLY422 4.8 27.2 1.0 C2 D:GOL802 4.8 43.6 1.0 C D:CYS420 4.8 23.4 1.0 N D:VAL421 4.9 28.8 1.0

H.Li, C.D.Hardy, C.T.Reidl, Q.Jing, F.Xue, M.Cinelli, R.B.Silverman, T.L.Poulos. Crystallographic and Computational Insights Into Isoform-Selective Dynamics in Nitric Oxide Synthase. Biochemistry 2024.
ISSN: ISSN 0006-2960
PubMed: 38417024
DOI: 10.1021/ACS.BIOCHEM.3C00601