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Iron in PDB 6pp0: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclobutylmethoxy)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-(Cyclobutylmethoxy)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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp0 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) 39.79 / 1.97
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.071, 152.948, 109.228, 90.00, 90.89, 90.00
R / Rfree (%) 20.7 / 26.1

Other elements in 6pp0:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclobutylmethoxy)Phenyl)-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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine (pdb code 6pp0). 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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp0:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6pp0

Go back to Iron Binding Sites List in 6pp0
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-(Cyclobutylmethoxy)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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:47.0
occ:1.00
 FE A:HEM501 0.0 47.0 1.0
ND A:HEM501 2.1 57.4 1.0
NA A:HEM501 2.1 60.3 1.0
NC A:HEM501 2.1 60.0 1.0
NB A:HEM501 2.1 50.4 1.0
SG A:CYS184 2.3 43.0 1.0
C1D A:HEM501 3.0 66.9 1.0
C4A A:HEM501 3.1 58.6 1.0
C4C A:HEM501 3.1 61.2 1.0
C1B A:HEM501 3.1 53.6 1.0
C4D A:HEM501 3.1 53.6 1.0
C1A A:HEM501 3.1 47.6 1.0
C4B A:HEM501 3.1 54.6 1.0
C1C A:HEM501 3.1 58.6 1.0
CB A:CYS184 3.2 47.2 1.0
CHD A:HEM501 3.4 66.9 1.0
CHB A:HEM501 3.4 57.6 1.0
CHA A:HEM501 3.5 43.0 1.0
CHC A:HEM501 3.5 48.4 1.0
C04 A:OUP503 3.8 54.3 1.0
C05 A:OUP503 4.0 54.9 1.0
CA A:CYS184 4.0 42.7 1.0
C03 A:OUP503 4.1 40.3 1.0
C4A A:OUP503 4.1 58.8 1.0
C2D A:HEM501 4.3 62.2 1.0
C3A A:HEM501 4.3 55.0 1.0
C2B A:HEM501 4.3 54.9 1.0
C3D A:HEM501 4.3 59.4 1.0
NE1 A:TRP178 4.3 51.4 1.0
C2A A:HEM501 4.3 50.4 1.0
C3C A:HEM501 4.3 60.6 1.0
C3B A:HEM501 4.3 58.1 1.0
C2C A:HEM501 4.4 61.0 1.0
C10 A:OUP503 4.4 53.2 1.0
C06 A:OUP503 4.4 54.2 1.0
C02 A:OUP503 4.5 46.5 1.0
N01 A:OUP503 4.6 36.1 1.0
C A:CYS184 4.8 42.3 1.0
N A:GLY186 4.9 37.4 1.0
CD1 A:TRP178 4.9 58.7 1.0

Iron binding site 2 out of 4 in 6pp0

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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-(Cyclobutylmethoxy)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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:31.4
occ:1.00
 FE B:HEM501 0.0 31.4 1.0
NB B:HEM501 2.0 39.5 1.0
ND B:HEM501 2.1 35.9 1.0
NA B:HEM501 2.1 35.5 1.0
NC B:HEM501 2.1 40.9 1.0
SG B:CYS184 2.2 28.5 1.0
C1B B:HEM501 3.0 34.2 1.0
C1D B:HEM501 3.0 35.4 1.0
C4A B:HEM501 3.1 40.7 1.0
C4C B:HEM501 3.1 41.5 1.0
C4B B:HEM501 3.1 44.0 1.0
C4D B:HEM501 3.1 50.2 1.0
C1A B:HEM501 3.2 30.7 1.0
C1C B:HEM501 3.2 39.1 1.0
CHB B:HEM501 3.3 30.9 1.0
CB B:CYS184 3.4 33.2 1.0
CHD B:HEM501 3.4 35.5 1.0
CHA B:HEM501 3.5 35.3 1.0
CHC B:HEM501 3.5 36.2 1.0
C04 B:OUP503 3.9 47.7 1.0
C05 B:OUP503 4.0 34.7 1.0
CA B:CYS184 4.1 34.7 1.0
C2B B:HEM501 4.2 39.3 1.0
C4A B:OUP503 4.3 33.2 1.0
C03 B:OUP503 4.3 31.6 1.0
C3B B:HEM501 4.3 39.2 1.0
C2D B:HEM501 4.3 43.2 1.0
C3A B:HEM501 4.3 35.3 1.0
C3D B:HEM501 4.3 47.2 1.0
C2A B:HEM501 4.3 41.2 1.0
C06 B:OUP503 4.4 37.0 1.0
C3C B:HEM501 4.4 37.6 1.0
C2C B:HEM501 4.4 36.9 1.0
C10 B:OUP503 4.4 40.1 1.0
NE1 B:TRP178 4.5 41.0 1.0
C02 B:OUP503 4.7 35.4 1.0
N01 B:OUP503 4.7 31.0 1.0
N B:GLY186 4.8 36.1 1.0
C B:CYS184 4.9 36.4 1.0

Iron binding site 3 out of 4 in 6pp0

Go back to Iron Binding Sites List in 6pp0
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-(Cyclobutylmethoxy)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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:39.6
occ:1.00
 FE C:HEM501 0.0 39.6 1.0
ND C:HEM501 2.1 45.8 1.0
NA C:HEM501 2.1 44.5 1.0
NC C:HEM501 2.1 36.1 1.0
NB C:HEM501 2.1 38.5 1.0
SG C:CYS184 2.3 38.9 1.0
C4D C:HEM501 3.1 46.4 1.0
C1A C:HEM501 3.1 40.9 1.0
C1D C:HEM501 3.1 50.1 1.0
C1C C:HEM501 3.1 49.2 1.0
C4A C:HEM501 3.1 43.8 1.0
C1B C:HEM501 3.1 44.0 1.0
C4B C:HEM501 3.1 42.8 1.0
C4C C:HEM501 3.2 41.9 1.0
CB C:CYS184 3.3 34.8 1.0
CHA C:HEM501 3.4 32.3 1.0
CHC C:HEM501 3.5 43.9 1.0
CHB C:HEM501 3.5 38.0 1.0
CHD C:HEM501 3.5 51.3 1.0
C04 C:OUP503 3.9 45.5 1.0
CA C:CYS184 4.0 34.9 1.0
C05 C:OUP503 4.0 45.6 1.0
C03 C:OUP503 4.1 41.7 1.0
C4A C:OUP503 4.3 45.9 1.0
C3D C:HEM501 4.3 45.4 1.0
C2D C:HEM501 4.3 42.3 1.0
C2A C:HEM501 4.3 43.6 1.0
C2B C:HEM501 4.3 47.7 1.0
C3A C:HEM501 4.3 44.1 1.0
C3B C:HEM501 4.3 49.5 1.0
C2C C:HEM501 4.4 52.8 1.0
NE1 C:TRP178 4.4 43.2 1.0
C3C C:HEM501 4.4 50.0 1.0
C10 C:OUP503 4.4 38.2 1.0
C06 C:OUP503 4.5 52.6 1.0
C02 C:OUP503 4.5 45.2 1.0
N01 C:OUP503 4.6 40.0 1.0
C C:CYS184 4.8 29.2 1.0
CD1 C:TRP178 4.9 41.3 1.0
N C:GLY186 4.9 34.2 1.0
N C:VAL185 5.0 34.1 1.0

Iron binding site 4 out of 4 in 6pp0

Go back to Iron Binding Sites List in 6pp0
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-(Cyclobutylmethoxy)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-(Cyclobutylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:32.3
occ:1.00
 FE D:HEM501 0.0 32.3 1.0
NA D:HEM501 2.0 35.5 1.0
ND D:HEM501 2.1 36.2 1.0
NB D:HEM501 2.1 28.7 1.0
NC D:HEM501 2.1 27.7 1.0
SG D:CYS184 2.3 27.8 1.0
C4A D:HEM501 3.0 33.7 1.0
C1D D:HEM501 3.1 39.4 1.0
C1B D:HEM501 3.1 35.3 1.0
C1A D:HEM501 3.1 34.7 1.0
C4C D:HEM501 3.1 34.3 1.0
C4D D:HEM501 3.1 33.0 1.0
C1C D:HEM501 3.2 39.2 1.0
C4B D:HEM501 3.2 41.4 1.0
CB D:CYS184 3.3 34.5 1.0
CHB D:HEM501 3.3 24.6 1.0
CHD D:HEM501 3.4 28.7 1.0
CHA D:HEM501 3.5 33.2 1.0
CHC D:HEM501 3.6 37.4 1.0
C04 D:OUP503 4.0 47.2 1.0
C05 D:OUP503 4.0 38.5 1.0
CA D:CYS184 4.1 34.4 1.0
C3A D:HEM501 4.2 41.2 1.0
C2A D:HEM501 4.3 34.4 1.0
C4A D:OUP503 4.3 41.8 1.0
C2D D:HEM501 4.3 42.3 1.0
C2B D:HEM501 4.3 35.3 1.0
C3D D:HEM501 4.3 41.0 1.0
C06 D:OUP503 4.3 29.5 1.0
C3C D:HEM501 4.3 41.4 1.0
C03 D:OUP503 4.4 34.1 1.0
C2C D:HEM501 4.4 35.0 1.0
C3B D:HEM501 4.4 40.5 1.0
NE1 D:TRP178 4.4 31.5 1.0
C10 D:OUP503 4.4 34.3 1.0
C02 D:OUP503 4.7 38.2 1.0
N01 D:OUP503 4.7 30.6 1.0
N D:GLY186 4.7 30.7 1.0
C D:CYS184 4.8 30.6 1.0
N D:VAL185 5.0 28.4 1.0
CD1 D:TRP178 5.0 31.3 1.0
C07 D:OUP503 5.0 37.5 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 06:23:59 2024

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