Iron in PDB 6poy: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine, PDB code: 6poy was solved by G.Chreifi, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 52.60 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.689, 153.410, 109.188, 90.00, 90.60, 90.00
R / Rfree (%) 19.8 / 26.1

Other elements in 6poy:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine also contains other interesting chemical elements:

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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine (pdb code 6poy). 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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine, PDB code: 6poy:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:50.0
occ:1.00
 FE A:HEM501 0.0 50.0 1.0
NB A:HEM501 2.1 56.0 1.0
NC A:HEM501 2.1 62.1 1.0
NA A:HEM501 2.1 52.3 1.0
ND A:HEM501 2.1 50.0 1.0
SG A:CYS184 2.3 37.3 1.0
C1B A:HEM501 3.0 63.1 1.0
C4A A:HEM501 3.0 54.7 1.0
C4C A:HEM501 3.1 62.5 1.0
C1D A:HEM501 3.1 57.3 1.0
C4B A:HEM501 3.1 53.7 1.0
C1C A:HEM501 3.1 57.9 1.0
C1A A:HEM501 3.1 47.0 1.0
C4D A:HEM501 3.2 56.8 1.0
CB A:CYS184 3.3 42.2 1.0
CHB A:HEM501 3.4 62.0 1.0
CHD A:HEM501 3.4 51.2 1.0
CHC A:HEM501 3.5 55.7 1.0
CHA A:HEM501 3.5 54.0 1.0
C04 A:OSG503 3.8 55.6 1.0
C05 A:OSG503 3.9 58.7 1.0
CA A:CYS184 4.0 42.9 1.0
C11 A:OSG503 4.0 58.0 1.0
C03 A:OSG503 4.1 48.8 1.0
C2B A:HEM501 4.3 55.2 1.0
C06 A:OSG503 4.3 57.8 1.0
C3A A:HEM501 4.3 56.6 1.0
C3B A:HEM501 4.3 50.2 1.0
C3C A:HEM501 4.3 63.5 1.0
C2A A:HEM501 4.3 60.0 1.0
C2C A:HEM501 4.3 62.4 1.0
C2D A:HEM501 4.3 57.2 1.0
C3D A:HEM501 4.4 62.5 1.0
C10 A:OSG503 4.4 54.3 1.0
NE1 A:TRP178 4.4 55.5 1.0
C02 A:OSG503 4.6 47.2 1.0
N01 A:OSG503 4.7 50.7 1.0
C A:CYS184 4.9 50.6 1.0
N A:GLY186 4.9 40.8 1.0
N A:VAL185 5.0 50.7 1.0
C07 A:OSG503 5.0 58.1 1.0

Iron binding site 2 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:29.2
occ:1.00
 FE B:HEM501 0.0 29.2 1.0
NA B:HEM501 2.0 42.9 1.0
NB B:HEM501 2.1 40.6 1.0
ND B:HEM501 2.2 42.1 1.0
NC B:HEM501 2.2 39.8 1.0
SG B:CYS184 2.2 22.3 1.0
C4A B:HEM501 3.0 35.4 1.0
C1B B:HEM501 3.0 36.0 1.0
C1A B:HEM501 3.1 34.4 1.0
C4B B:HEM501 3.1 37.5 1.0
C1D B:HEM501 3.1 37.3 1.0
C4D B:HEM501 3.2 43.1 1.0
C4C B:HEM501 3.2 32.2 1.0
C1C B:HEM501 3.2 40.2 1.0
CHB B:HEM501 3.3 24.8 1.0
CB B:CYS184 3.3 22.1 1.0
CHD B:HEM501 3.5 32.0 1.0
CHC B:HEM501 3.5 36.0 1.0
CHA B:HEM501 3.5 35.9 1.0
C04 B:OSG503 4.0 35.7 1.0
C05 B:OSG503 4.0 28.0 1.0
CA B:CYS184 4.1 34.7 1.0
C3A B:HEM501 4.2 34.3 1.0
C2B B:HEM501 4.3 42.1 1.0
C2A B:HEM501 4.3 38.8 1.0
C11 B:OSG503 4.3 35.2 1.0
C03 B:OSG503 4.3 19.9 1.0
C3B B:HEM501 4.3 37.5 1.0
C06 B:OSG503 4.3 28.8 1.0
C2D B:HEM501 4.4 34.0 1.0
C3D B:HEM501 4.4 32.2 1.0
NE1 B:TRP178 4.4 27.1 1.0
C2C B:HEM501 4.4 42.2 1.0
C3C B:HEM501 4.4 41.6 1.0
C10 B:OSG503 4.4 34.6 1.0
C02 B:OSG503 4.7 25.2 1.0
N01 B:OSG503 4.8 31.8 1.0
N B:GLY186 4.8 24.7 1.0
C B:CYS184 4.8 31.1 1.0
N B:VAL185 4.9 27.1 1.0
C07 B:OSG503 5.0 27.6 1.0

Iron binding site 3 out of 4 in 6poy

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Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:37.5
occ:1.00
 FE C:HEM501 0.0 37.5 1.0
ND C:HEM501 2.0 43.3 1.0
NA C:HEM501 2.1 46.2 1.0
NB C:HEM501 2.1 41.8 1.0
NC C:HEM501 2.1 48.7 1.0
SG C:CYS184 2.4 34.4 1.0
C4D C:HEM501 3.0 43.7 1.0
C1A C:HEM501 3.1 36.5 1.0
C4B C:HEM501 3.1 49.2 1.0
C4A C:HEM501 3.1 37.6 1.0
C1C C:HEM501 3.1 52.2 1.0
C1B C:HEM501 3.1 40.7 1.0
C1D C:HEM501 3.1 44.7 1.0
C4C C:HEM501 3.2 45.5 1.0
CHA C:HEM501 3.4 36.1 1.0
CB C:CYS184 3.4 31.5 1.0
CHC C:HEM501 3.4 49.4 1.0
CHB C:HEM501 3.5 27.5 1.0
CHD C:HEM501 3.5 38.2 1.0
C04 C:OSG503 3.8 47.7 1.0
C05 C:OSG503 4.0 41.7 1.0
C03 C:OSG503 4.0 48.5 1.0
C11 C:OSG503 4.1 42.7 1.0
CA C:CYS184 4.1 30.4 1.0
C3D C:HEM501 4.3 41.0 1.0
C2A C:HEM501 4.3 41.3 1.0
C2D C:HEM501 4.3 33.1 1.0
C3A C:HEM501 4.3 37.4 1.0
C2B C:HEM501 4.3 38.8 1.0
C3B C:HEM501 4.3 42.0 1.0
C2C C:HEM501 4.3 51.6 1.0
NE1 C:TRP178 4.4 46.0 1.0
C3C C:HEM501 4.4 41.4 1.0
C06 C:OSG503 4.4 40.3 1.0
C10 C:OSG503 4.4 36.4 1.0
C02 C:OSG503 4.5 40.6 1.0
N01 C:OSG503 4.7 37.6 1.0
N C:GLY186 4.9 34.1 1.0
C C:CYS184 4.9 30.4 1.0
CD1 C:TRP178 4.9 38.4 1.0

Iron binding site 4 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:20.5
occ:1.00
 FE D:HEM501 0.0 20.5 1.0
NA D:HEM501 2.0 38.9 1.0
ND D:HEM501 2.1 37.8 1.0
NB D:HEM501 2.2 31.7 1.0
NC D:HEM501 2.2 30.3 1.0
SG D:CYS184 2.2 19.9 1.0
C4A D:HEM501 3.0 32.7 1.0
C1A D:HEM501 3.0 43.4 1.0
C1B D:HEM501 3.1 34.6 1.0
C1D D:HEM501 3.1 33.7 1.0
C4D D:HEM501 3.1 44.4 1.0
C4C D:HEM501 3.2 32.1 1.0
C1C D:HEM501 3.2 40.5 1.0
C4B D:HEM501 3.2 30.7 1.0
CB D:CYS184 3.3 19.9 1.0
CHB D:HEM501 3.4 22.9 1.0
CHD D:HEM501 3.5 34.2 1.0
CHA D:HEM501 3.5 33.1 1.0
CHC D:HEM501 3.6 40.9 1.0
C04 D:OSG503 3.9 40.6 1.0
C05 D:OSG503 4.0 36.7 1.0
CA D:CYS184 4.0 28.1 1.0
C3A D:HEM501 4.2 39.0 1.0
C2A D:HEM501 4.2 35.4 1.0
C03 D:OSG503 4.2 31.6 1.0
C11 D:OSG503 4.3 37.4 1.0
C10 D:OSG503 4.3 34.2 1.0
C06 D:OSG503 4.3 36.2 1.0
C2D D:HEM501 4.3 32.5 1.0
C2B D:HEM501 4.4 38.8 1.0
C3D D:HEM501 4.4 33.7 1.0
C3C D:HEM501 4.4 42.6 1.0
C3B D:HEM501 4.4 36.1 1.0
C2C D:HEM501 4.4 36.6 1.0
C02 D:OSG503 4.6 34.1 1.0
NE1 D:TRP178 4.6 35.2 1.0
N01 D:OSG503 4.6 24.8 1.0
C D:CYS184 4.8 22.5 1.0
N D:GLY186 4.8 24.0 1.0
N D:VAL185 4.9 29.6 1.0
C07 D:OSG503 5.0 36.4 1.0

Reference:

M.A.Cinelli, C.T.Reidl, H.Li, G.Chreifi, T.L.Poulos, R.B.Silverman. First Contact: 7-Phenyl-2-Aminoquinolines, Potent and Selective Neuronal Nitric Oxide Synthase Inhibitors That Target An Isoform-Specific Aspartate. J.Med.Chem. 2020.
ISSN: ISSN 0022-2623
PubMed: 32302123
DOI: 10.1021/ACS.JMEDCHEM.9B01573
Page generated: Sun Dec 13 16:49:34 2020

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