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Iron in PDB 6pp3: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Pyridin-2-Ylmethoxy)Phenyl)-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-(Pyridin-2-Ylmethoxy)Phenyl)-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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp3 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) 49.86 / 1.95
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.872, 152.078, 108.580, 90.00, 90.91, 90.00
R / Rfree (%) 21.1 / 26

Other elements in 6pp3:

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

Chlorine (Cl) 4 atoms
Gadolinium (Gd) 4 atoms
Zinc (Zn) 2 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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine (pdb code 6pp3). 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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp3:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6pp3

Go back to Iron Binding Sites List in 6pp3
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-(Pyridin-2-Ylmethoxy)Phenyl)-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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:51.7
occ:1.00
 FE A:HEM501 0.0 51.7 1.0
ND A:HEM501 2.0 62.0 1.0
NC A:HEM501 2.1 66.7 1.0
NA A:HEM501 2.1 53.0 1.0
NB A:HEM501 2.1 52.3 1.0
SG A:CYS184 2.3 46.4 1.0
C1D A:HEM501 3.0 69.5 1.0
C4C A:HEM501 3.0 71.3 1.0
C4D A:HEM501 3.1 58.0 1.0
C1C A:HEM501 3.1 69.7 1.0
C4A A:HEM501 3.1 52.1 1.0
C1A A:HEM501 3.1 52.4 1.0
C1B A:HEM501 3.1 52.7 1.0
C4B A:HEM501 3.1 65.1 1.0
CB A:CYS184 3.3 38.5 1.0
C4A A:OS7503 3.4 94.5 1.0
CHD A:HEM501 3.4 71.2 1.0
CHA A:HEM501 3.5 53.7 1.0
CHC A:HEM501 3.5 71.9 1.0
CHB A:HEM501 3.5 46.7 1.0
C04 A:OS7503 3.5 90.0 1.0
C03 A:OS7503 3.8 74.6 1.0
C05 A:OS7503 4.1 0.4 1.0
CA A:CYS184 4.1 40.6 1.0
C2D A:HEM501 4.2 65.2 1.0
C3C A:HEM501 4.3 68.5 1.0
C3D A:HEM501 4.3 58.3 1.0
C2C A:HEM501 4.3 67.0 1.0
C3A A:HEM501 4.3 52.6 1.0
C2B A:HEM501 4.3 48.9 1.0
C2A A:HEM501 4.3 56.1 1.0
C3B A:HEM501 4.4 57.3 1.0
C06 A:OS7503 4.4 0.8 1.0
C02 A:OS7503 4.6 71.9 1.0
NE1 A:TRP178 4.6 53.5 1.0
C10 A:OS7503 4.8 98.7 1.0
C A:CYS184 4.9 42.6 1.0
N A:GLY186 4.9 44.5 1.0

Iron binding site 2 out of 4 in 6pp3

Go back to Iron Binding Sites List in 6pp3
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-(Pyridin-2-Ylmethoxy)Phenyl)-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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:31.3
occ:1.00
 FE B:HEM501 0.0 31.3 1.0
ND B:HEM501 2.0 36.9 1.0
NB B:HEM501 2.1 37.5 1.0
NC B:HEM501 2.1 29.6 1.0
NA B:HEM501 2.1 26.1 1.0
SG B:CYS184 2.4 30.4 1.0
C1D B:HEM501 3.0 30.2 1.0
C1B B:HEM501 3.0 37.5 1.0
C4C B:HEM501 3.0 35.5 1.0
C4D B:HEM501 3.1 36.2 1.0
C4A B:HEM501 3.1 31.0 1.0
C4B B:HEM501 3.1 41.7 1.0
C1A B:HEM501 3.2 21.6 1.0
C1C B:HEM501 3.2 33.6 1.0
CB B:CYS184 3.3 29.0 1.0
CHD B:HEM501 3.3 32.3 1.0
C4A B:OS7503 3.3 65.1 1.0
CHB B:HEM501 3.4 32.5 1.0
CHA B:HEM501 3.5 30.8 1.0
CHC B:HEM501 3.5 34.5 1.0
C04 B:OS7503 3.6 57.3 1.0
C03 B:OS7503 3.9 58.4 1.0
CA B:CYS184 4.0 29.5 1.0
C05 B:OS7503 4.2 63.5 1.0
C2D B:HEM501 4.2 27.6 1.0
C3D B:HEM501 4.3 34.0 1.0
C2B B:HEM501 4.3 39.4 1.0
C3C B:HEM501 4.3 26.9 1.0
C3B B:HEM501 4.3 35.6 1.0
NE1 B:TRP178 4.3 36.7 1.0
C3A B:HEM501 4.3 37.5 1.0
C2C B:HEM501 4.4 31.7 1.0
C2A B:HEM501 4.4 34.5 1.0
C06 B:OS7503 4.5 68.7 1.0
C02 B:OS7503 4.8 61.8 1.0
C B:CYS184 4.8 25.1 1.0
N B:GLY186 4.8 37.0 1.0
N B:VAL185 4.9 33.4 1.0

Iron binding site 3 out of 4 in 6pp3

Go back to Iron Binding Sites List in 6pp3
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-(Pyridin-2-Ylmethoxy)Phenyl)-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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:42.1
occ:1.00
 FE C:HEM501 0.0 42.1 1.0
NC C:HEM501 2.0 48.3 1.0
NB C:HEM501 2.1 45.4 1.0
ND C:HEM501 2.1 39.5 1.0
NA C:HEM501 2.1 47.8 1.0
SG C:CYS184 2.3 41.0 1.0
C1C C:HEM501 3.0 50.8 1.0
C4B C:HEM501 3.0 37.1 1.0
C4D C:HEM501 3.1 39.9 1.0
C4C C:HEM501 3.1 49.5 1.0
C1A C:HEM501 3.1 43.3 1.0
C4A C:HEM501 3.1 42.4 1.0
C1B C:HEM501 3.2 45.0 1.0
C1D C:HEM501 3.2 43.4 1.0
CHC C:HEM501 3.3 44.2 1.0
CB C:CYS184 3.4 40.9 1.0
CHA C:HEM501 3.4 34.2 1.0
CHD C:HEM501 3.5 48.3 1.0
CHB C:HEM501 3.5 44.4 1.0
C4A C:OS7503 3.8 78.6 1.0
C04 C:OS7503 3.9 75.5 1.0
CA C:CYS184 4.1 40.4 1.0
C03 C:OS7503 4.2 70.5 1.0
C05 C:OS7503 4.3 88.2 1.0
C2C C:HEM501 4.3 47.6 1.0
C3B C:HEM501 4.3 43.1 1.0
C3C C:HEM501 4.3 43.4 1.0
C3D C:HEM501 4.3 39.2 1.0
C2B C:HEM501 4.3 43.7 1.0
C2A C:HEM501 4.3 45.2 1.0
C3A C:HEM501 4.4 44.9 1.0
C2D C:HEM501 4.4 39.8 1.0
NE1 C:TRP178 4.4 44.1 1.0
C06 C:OS7503 4.6 97.9 1.0
N C:GLY186 4.9 33.9 1.0
C C:CYS184 4.9 31.3 1.0
C02 C:OS7503 4.9 71.9 1.0
CD1 C:TRP178 4.9 35.5 1.0
C10 C:OS7503 4.9 86.1 1.0

Iron binding site 4 out of 4 in 6pp3

Go back to Iron Binding Sites List in 6pp3
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-(Pyridin-2-Ylmethoxy)Phenyl)-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-(Pyridin-2-Ylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:30.8
occ:1.00
 FE D:HEM501 0.0 30.8 1.0
NA D:HEM501 2.0 34.1 1.0
ND D:HEM501 2.1 36.8 1.0
NB D:HEM501 2.1 31.7 1.0
SG D:CYS184 2.2 31.5 1.0
NC D:HEM501 2.2 28.6 1.0
C4A D:HEM501 3.0 28.3 1.0
C1B D:HEM501 3.0 38.1 1.0
C1D D:HEM501 3.0 40.6 1.0
C1A D:HEM501 3.1 27.9 1.0
C4D D:HEM501 3.1 33.4 1.0
C4C D:HEM501 3.1 36.5 1.0
C4B D:HEM501 3.2 28.5 1.0
C1C D:HEM501 3.2 34.0 1.0
CHB D:HEM501 3.3 27.0 1.0
CB D:CYS184 3.3 32.8 1.0
CHD D:HEM501 3.4 38.9 1.0
C4A D:OS7503 3.5 71.3 1.0
CHA D:HEM501 3.5 32.0 1.0
CHC D:HEM501 3.6 34.7 1.0
C04 D:OS7503 3.6 64.8 1.0
C03 D:OS7503 3.9 45.8 1.0
CA D:CYS184 4.1 22.3 1.0
C05 D:OS7503 4.2 74.3 1.0
C3A D:HEM501 4.2 33.1 1.0
C2B D:HEM501 4.3 35.8 1.0
C2D D:HEM501 4.3 40.6 1.0
C2A D:HEM501 4.3 30.9 1.0
C3D D:HEM501 4.3 38.8 1.0
C3B D:HEM501 4.3 36.9 1.0
C3C D:HEM501 4.4 30.1 1.0
C2C D:HEM501 4.4 36.1 1.0
NE1 D:TRP178 4.5 41.6 1.0
C06 D:OS7503 4.6 78.8 1.0
N D:GLY186 4.6 29.4 1.0
C02 D:OS7503 4.7 55.7 1.0
C D:CYS184 4.8 26.9 1.0
CA D:GLY186 4.9 26.7 1.0
C10 D:OS7503 4.9 70.8 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: Wed Aug 7 06:29:13 2024

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