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Iron in PDB 6pp1: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclopropylmethoxy)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-(Cyclopropylmethoxy)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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp1 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) 49.71 / 1.76
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.585, 153.030, 108.781, 90.00, 90.78, 90.00
R / Rfree (%) 18 / 21.2

Other elements in 6pp1:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclopropylmethoxy)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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine (pdb code 6pp1). 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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp1:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6pp1

Go back to Iron Binding Sites List in 6pp1
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-(Cyclopropylmethoxy)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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:48.9
occ:1.00
 FE A:HEM501 0.0 48.9 1.0
ND A:HEM501 2.1 47.8 1.0
NA A:HEM501 2.1 45.7 1.0
NC A:HEM501 2.1 43.5 1.0
NB A:HEM501 2.1 47.2 1.0
SG A:CYS184 2.3 41.0 1.0
C4D A:HEM501 3.1 51.8 1.0
C1A A:HEM501 3.1 42.6 1.0
C1C A:HEM501 3.1 55.1 1.0
C4B A:HEM501 3.1 55.4 1.0
C1D A:HEM501 3.1 54.7 1.0
C4A A:HEM501 3.1 45.6 1.0
C1B A:HEM501 3.1 51.2 1.0
C4C A:HEM501 3.1 54.4 1.0
CHA A:HEM501 3.4 40.5 1.0
CHC A:HEM501 3.4 47.8 1.0
CB A:CYS184 3.4 38.0 1.0
CHB A:HEM501 3.5 44.9 1.0
CHD A:HEM501 3.5 52.9 1.0
C04 A:OU1503 3.6 66.7 1.0
C05 A:OU1503 3.9 71.5 1.0
C11 A:OU1503 3.9 65.4 1.0
C03 A:OU1503 4.0 57.6 1.0
CA A:CYS184 4.2 35.0 1.0
C3D A:HEM501 4.3 52.9 1.0
C06 A:OU1503 4.3 74.3 1.0
C2D A:HEM501 4.3 55.9 1.0
C2A A:HEM501 4.3 45.1 1.0
C2B A:HEM501 4.3 48.6 1.0
C3B A:HEM501 4.3 54.4 1.0
C3A A:HEM501 4.3 45.0 1.0
C2C A:HEM501 4.3 53.9 1.0
C3C A:HEM501 4.3 56.6 1.0
NE1 A:TRP178 4.3 49.7 1.0
C10 A:OU1503 4.4 65.0 1.0
C02 A:OU1503 4.5 52.2 1.0
N01 A:OU1503 4.7 51.7 1.0
N A:GLY186 4.9 40.5 1.0
C A:CYS184 5.0 41.2 1.0
CD1 A:TRP178 5.0 48.0 1.0

Iron binding site 2 out of 4 in 6pp1

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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-(Cyclopropylmethoxy)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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:28.2
occ:1.00
 FE B:HEM502 0.0 28.2 1.0
ND B:HEM502 2.1 31.1 1.0
NC B:HEM502 2.1 25.9 1.0
NA B:HEM502 2.1 28.0 1.0
NB B:HEM502 2.1 33.2 1.0
SG B:CYS184 2.3 28.7 1.0
C1D B:HEM502 3.1 28.3 1.0
C1C B:HEM502 3.1 26.1 1.0
C1A B:HEM502 3.1 22.6 1.0
C4D B:HEM502 3.1 30.8 1.0
C4A B:HEM502 3.1 29.8 1.0
C4C B:HEM502 3.1 30.5 1.0
C1B B:HEM502 3.1 27.5 1.0
C4B B:HEM502 3.1 26.4 1.0
CB B:CYS184 3.4 24.6 1.0
CHA B:HEM502 3.4 25.9 1.0
CHD B:HEM502 3.5 29.1 1.0
CHC B:HEM502 3.5 28.9 1.0
CHB B:HEM502 3.5 25.7 1.0
C04 B:OU1504 3.8 36.7 1.0
C05 B:OU1504 4.0 44.4 1.0
CA B:CYS184 4.1 25.0 1.0
C11 B:OU1504 4.1 35.5 1.0
C03 B:OU1504 4.1 33.1 1.0
C2D B:HEM502 4.3 30.8 1.0
NE1 B:TRP178 4.3 29.5 1.0
C3D B:HEM502 4.3 31.1 1.0
C2C B:HEM502 4.3 25.2 1.0
C2A B:HEM502 4.3 26.8 1.0
C3A B:HEM502 4.3 28.6 1.0
C3C B:HEM502 4.3 24.4 1.0
C2B B:HEM502 4.4 27.4 1.0
C3B B:HEM502 4.4 28.2 1.0
C06 B:OU1504 4.4 45.4 1.0
C10 B:OU1504 4.5 46.9 1.0
C02 B:OU1504 4.6 32.1 1.0
N01 B:OU1504 4.8 36.4 1.0
N B:GLY186 4.8 32.6 1.0
C B:CYS184 4.8 26.6 1.0
CD1 B:TRP178 4.9 27.5 1.0
N B:VAL185 4.9 27.9 1.0

Iron binding site 3 out of 4 in 6pp1

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

b:37.8
occ:1.00
 FE C:HEM501 0.0 37.8 1.0
ND C:HEM501 2.1 43.9 1.0
NB C:HEM501 2.1 42.4 1.0
NC C:HEM501 2.1 40.3 1.0
NA C:HEM501 2.1 38.7 1.0
SG C:CYS184 2.4 38.9 1.0
C4B C:HEM501 3.1 43.6 1.0
C4D C:HEM501 3.1 42.5 1.0
C1D C:HEM501 3.1 45.6 1.0
C1C C:HEM501 3.1 43.5 1.0
C1B C:HEM501 3.1 38.6 1.0
C4C C:HEM501 3.1 42.1 1.0
C1A C:HEM501 3.1 41.7 1.0
C4A C:HEM501 3.1 36.3 1.0
CHC C:HEM501 3.4 40.0 1.0
CHA C:HEM501 3.5 33.4 1.0
CHD C:HEM501 3.5 46.4 1.0
CB C:CYS184 3.5 31.5 1.0
CHB C:HEM501 3.5 36.5 1.0
C04 C:OU1503 3.8 56.4 1.0
C03 C:OU1503 4.0 50.2 1.0
C11 C:OU1503 4.1 64.6 1.0
C05 C:OU1503 4.1 63.3 1.0
CA C:CYS184 4.1 34.3 1.0
C3B C:HEM501 4.3 42.7 1.0
C2B C:HEM501 4.3 38.7 1.0
C3D C:HEM501 4.3 43.9 1.0
C2D C:HEM501 4.3 42.7 1.0
C2C C:HEM501 4.3 44.6 1.0
C3C C:HEM501 4.3 41.8 1.0
C2A C:HEM501 4.4 45.7 1.0
C3A C:HEM501 4.4 39.6 1.0
NE1 C:TRP178 4.4 39.4 1.0
C02 C:OU1503 4.5 49.5 1.0
C10 C:OU1503 4.6 57.3 1.0
C06 C:OU1503 4.6 66.1 1.0
N01 C:OU1503 4.7 49.6 1.0
N C:GLY186 4.8 36.1 1.0
C C:CYS184 4.9 31.2 1.0
N C:VAL185 5.0 33.8 1.0

Iron binding site 4 out of 4 in 6pp1

Go back to Iron Binding Sites List in 6pp1
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-(Cyclopropylmethoxy)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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe502

b:27.6
occ:1.00
 FE D:HEM502 0.0 27.6 1.0
NA D:HEM502 2.0 26.1 1.0
ND D:HEM502 2.0 29.7 1.0
NC D:HEM502 2.1 23.9 1.0
NB D:HEM502 2.1 28.8 1.0
SG D:CYS184 2.3 25.3 1.0
C1D D:HEM502 3.0 26.8 1.0
C4A D:HEM502 3.1 28.3 1.0
C1A D:HEM502 3.1 26.4 1.0
C4C D:HEM502 3.1 26.3 1.0
C1C D:HEM502 3.1 26.5 1.0
C4D D:HEM502 3.1 23.0 1.0
C1B D:HEM502 3.1 29.8 1.0
C4B D:HEM502 3.1 25.0 1.0
CB D:CYS184 3.3 26.6 1.0
CHD D:HEM502 3.4 27.1 1.0
CHB D:HEM502 3.4 27.6 1.0
CHC D:HEM502 3.5 27.0 1.0
CHA D:HEM502 3.5 24.0 1.0
C04 D:OU1504 3.9 37.5 1.0
C05 D:OU1504 4.0 35.6 1.0
CA D:CYS184 4.1 23.5 1.0
C11 D:OU1504 4.2 38.8 1.0
C03 D:OU1504 4.2 35.7 1.0
C2D D:HEM502 4.3 28.7 1.0
C3A D:HEM502 4.3 28.2 1.0
C2A D:HEM502 4.3 26.5 1.0
C3D D:HEM502 4.3 30.5 1.0
C3C D:HEM502 4.3 25.9 1.0
C06 D:OU1504 4.3 39.5 1.0
C2C D:HEM502 4.3 28.7 1.0
C2B D:HEM502 4.3 27.7 1.0
NE1 D:TRP178 4.4 28.6 1.0
C3B D:HEM502 4.4 29.3 1.0
C10 D:OU1504 4.4 38.5 1.0
C02 D:OU1504 4.6 34.0 1.0
N01 D:OU1504 4.7 36.6 1.0
N D:GLY186 4.8 28.2 1.0
C D:CYS184 4.8 26.4 1.0
CD1 D:TRP178 5.0 28.0 1.0
C07 D:OU1504 5.0 44.2 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 06:24:03 2024

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