Atomistry » Iron » PDB 6ajo-6ayc » 6av6
Atomistry »
  Iron »
    PDB 6ajo-6ayc »
      6av6 »

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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy