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Iron in PDB 6av6: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine, PDB code: 6av6 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) 39.13 / 2.08
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.643, 152.780, 108.882, 90.00, 90.78, 90.00
R / Rfree (%) 19.4 / 23.9

Other elements in 6av6:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine also contains other interesting chemical elements:

Fluorine (F) 4 atoms
Zinc (Zn) 2 atoms
Gadolinium (Gd) 4 atoms
Chlorine (Cl) 4 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine (pdb code 6av6). 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 Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine, PDB code: 6av6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6av6

Go back to Iron Binding Sites List in 6av6
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-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 Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:54.8
occ:1.00
 FE A:HEM501 0.0 54.8 1.0
NA A:HEM501 2.0 59.2 1.0
NC A:HEM501 2.1 86.5 1.0
NB A:HEM501 2.1 61.7 1.0
ND A:HEM501 2.1 74.0 1.0
SG A:CYS184 2.3 46.5 1.0
C4A A:HEM501 3.1 64.3 1.0
C1A A:HEM501 3.1 62.7 1.0
C1C A:HEM501 3.1 79.5 1.0
C1B A:HEM501 3.1 66.0 1.0
C4C A:HEM501 3.1 85.5 1.0
C4B A:HEM501 3.1 71.3 1.0
C4D A:HEM501 3.1 72.9 1.0
C1D A:HEM501 3.1 82.7 1.0
CHA A:HEM501 3.4 69.1 1.0
CHB A:HEM501 3.4 64.7 1.0
CHC A:HEM501 3.4 73.0 1.0
CHD A:HEM501 3.5 86.7 1.0
CB A:CYS184 3.5 52.6 1.0
C04 A:W68502 3.9 67.3 1.0
C03 A:W68502 4.0 63.1 1.0
C07 A:W68502 4.2 61.2 1.0
CA A:CYS184 4.2 47.5 1.0
C05 A:W68502 4.2 71.0 1.0
C3A A:HEM501 4.3 64.9 1.0
C2A A:HEM501 4.3 73.0 1.0
C2C A:HEM501 4.3 80.3 1.0
C2B A:HEM501 4.3 61.9 1.0
C3C A:HEM501 4.3 83.7 1.0
C3B A:HEM501 4.3 71.1 1.0
C3D A:HEM501 4.4 74.2 1.0
C2D A:HEM501 4.4 71.8 1.0
C02 A:W68502 4.4 60.4 1.0
C06 A:W68502 4.6 69.2 1.0
NE1 A:TRP178 4.7 63.5 1.0
N01 A:W68502 4.7 67.8 1.0

Iron binding site 2 out of 4 in 6av6

Go back to Iron Binding Sites List in 6av6
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-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 Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:34.3
occ:1.00
 FE B:HEM502 0.0 34.3 1.0
NB B:HEM502 2.1 49.3 1.0
ND B:HEM502 2.1 35.0 1.0
NA B:HEM502 2.1 32.8 1.0
NC B:HEM502 2.1 31.6 1.0
SG B:CYS184 2.3 31.7 1.0
C1B B:HEM502 3.0 40.2 1.0
C4A B:HEM502 3.1 39.7 1.0
C4D B:HEM502 3.1 41.6 1.0
C1D B:HEM502 3.1 41.2 1.0
C4B B:HEM502 3.1 47.1 1.0
C4C B:HEM502 3.1 32.6 1.0
C1C B:HEM502 3.1 41.9 1.0
C1A B:HEM502 3.1 39.2 1.0
CHB B:HEM502 3.4 34.8 1.0
CHD B:HEM502 3.4 30.2 1.0
CB B:CYS184 3.4 29.2 1.0
CHA B:HEM502 3.5 30.7 1.0
CHC B:HEM502 3.5 38.4 1.0
C03 B:W68504 4.1 31.3 1.0
C04 B:W68504 4.1 42.1 1.0
CA B:CYS184 4.1 37.1 1.0
C2B B:HEM502 4.2 44.0 1.0
C3B B:HEM502 4.3 34.8 1.0
C3D B:HEM502 4.3 36.1 1.0
C2D B:HEM502 4.3 37.4 1.0
C3A B:HEM502 4.3 42.3 1.0
C3C B:HEM502 4.4 35.7 1.0
C2C B:HEM502 4.4 35.9 1.0
C2A B:HEM502 4.4 45.2 1.0
NE1 B:TRP178 4.4 35.8 1.0
C02 B:W68504 4.4 35.2 1.0
C05 B:W68504 4.5 36.9 1.0
C07 B:W68504 4.5 37.9 1.0
N01 B:W68504 4.8 36.0 1.0
C06 B:W68504 4.8 45.0 1.0
N B:GLY186 4.8 34.8 1.0
C B:CYS184 4.9 35.7 1.0
N B:VAL185 4.9 31.2 1.0

Iron binding site 3 out of 4 in 6av6

Go back to Iron Binding Sites List in 6av6
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine


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 Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:44.6
occ:1.00
 FE C:HEM501 0.0 44.6 1.0
NC C:HEM501 2.1 59.9 1.0
NA C:HEM501 2.1 50.8 1.0
ND C:HEM501 2.1 44.6 1.0
NB C:HEM501 2.1 59.7 1.0
SG C:CYS184 2.3 42.5 1.0
C1C C:HEM501 3.1 64.6 1.0
C1A C:HEM501 3.1 46.8 1.0
C4D C:HEM501 3.1 48.3 1.0
C4B C:HEM501 3.1 53.0 1.0
C4A C:HEM501 3.1 50.8 1.0
C4C C:HEM501 3.1 62.6 1.0
C1B C:HEM501 3.1 53.0 1.0
C1D C:HEM501 3.1 50.0 1.0
CB C:CYS184 3.4 46.5 1.0
CHA C:HEM501 3.4 35.7 1.0
CHC C:HEM501 3.4 55.6 1.0
CHD C:HEM501 3.5 54.7 1.0
CHB C:HEM501 3.5 39.0 1.0
CA C:CYS184 4.1 43.5 1.0
C03 C:W68503 4.1 51.9 1.0
C04 C:W68503 4.2 61.1 1.0
C2C C:HEM501 4.3 67.4 1.0
C3A C:HEM501 4.3 46.1 1.0
C3B C:HEM501 4.3 55.5 1.0
C2A C:HEM501 4.3 55.4 1.0
C2B C:HEM501 4.3 49.2 1.0
C3C C:HEM501 4.3 68.7 1.0
C3D C:HEM501 4.3 51.7 1.0
C2D C:HEM501 4.4 47.9 1.0
C02 C:W68503 4.4 53.6 1.0
NE1 C:TRP178 4.5 52.1 1.0
C05 C:W68503 4.6 62.8 1.0
C07 C:W68503 4.6 60.4 1.0
N01 C:W68503 4.7 58.1 1.0
C C:CYS184 4.8 36.0 1.0
C06 C:W68503 4.8 63.1 1.0
N C:GLY186 4.8 47.9 1.0
N C:VAL185 4.9 35.3 1.0
N02 C:W68503 4.9 46.9 1.0

Iron binding site 4 out of 4 in 6av6

Go back to Iron Binding Sites List in 6av6
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine


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 Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(3-Fluoro-5-(3-(Methylamino)Propyl)Phenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:33.0
occ:1.00
 FE D:HEM501 0.0 33.0 1.0
ND D:HEM501 2.1 34.9 1.0
NB D:HEM501 2.1 38.8 1.0
NA D:HEM501 2.1 30.8 1.0
NC D:HEM501 2.2 26.4 1.0
SG D:CYS184 2.2 30.1 1.0
C4A D:HEM501 3.0 30.8 1.0
C1B D:HEM501 3.0 38.3 1.0
C1D D:HEM501 3.1 34.1 1.0
C4D D:HEM501 3.1 38.1 1.0
C4C D:HEM501 3.1 31.1 1.0
C4B D:HEM501 3.1 34.3 1.0
C1A D:HEM501 3.2 38.3 1.0
C1C D:HEM501 3.2 30.0 1.0
CHB D:HEM501 3.3 28.9 1.0
CB D:CYS184 3.4 27.3 1.0
CHD D:HEM501 3.4 26.6 1.0
CHA D:HEM501 3.5 31.1 1.0
CHC D:HEM501 3.5 40.6 1.0
C04 D:W68503 4.0 31.2 1.0
C03 D:W68503 4.0 23.2 1.0
CA D:CYS184 4.2 28.1 1.0
C07 D:W68503 4.2 28.8 1.0
C3A D:HEM501 4.3 38.9 1.0
C2B D:HEM501 4.3 40.9 1.0
C2D D:HEM501 4.3 32.0 1.0
C3B D:HEM501 4.3 37.8 1.0
C3D D:HEM501 4.3 36.8 1.0
C2A D:HEM501 4.3 43.1 1.0
C3C D:HEM501 4.4 34.1 1.0
C2C D:HEM501 4.4 34.2 1.0
NE1 D:TRP178 4.4 37.4 1.0
C05 D:W68503 4.5 40.3 1.0
C02 D:W68503 4.5 36.7 1.0
N D:GLY186 4.8 27.2 1.0
C D:CYS184 4.9 30.1 1.0
C06 D:W68503 4.9 45.9 1.0
N01 D:W68503 4.9 35.7 1.0

Reference:

H.T.Do, H.Y.Wang, H.Li, G.Chreifi, T.L.Poulos, R.B.Silverman. Improvement of Cell Permeability of Human Neuronal Nitric Oxide Synthase Inhibitors Using Potent and Selective 2-Aminopyridine-Based Scaffolds with A Fluorobenzene Linker. J. Med. Chem. V. 60 9360 2017.
ISSN: ISSN 1520-4804
PubMed: 29091437
DOI: 10.1021/ACS.JMEDCHEM.7B01356
Page generated: Tue Aug 6 13:53:33 2024

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