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Iron in PDB 7tsi: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine, PDB code: 7tsi 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) 49.11 / 2.10
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.924, 151.386, 107.476, 90, 90.62, 90
R / Rfree (%) 21.7 / 27.7

Other elements in 7tsi:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine also contains other interesting chemical elements:

Gadolinium (Gd) 4 atoms
Chlorine (Cl) 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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine (pdb code 7tsi). 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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine, PDB code: 7tsi:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 7tsi

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

b:46.9
occ:1.00
 FE A:HEM501 0.0 46.9 1.0
NC A:HEM501 2.1 63.0 1.0
ND A:HEM501 2.1 49.2 1.0
NA A:HEM501 2.1 51.3 1.0
NB A:HEM501 2.1 54.5 1.0
SG A:CYS184 2.3 42.2 1.0
C1D A:HEM501 3.1 60.8 1.0
C4C A:HEM501 3.1 66.2 1.0
C4D A:HEM501 3.1 55.8 1.0
C1C A:HEM501 3.1 61.4 1.0
C1A A:HEM501 3.1 56.4 1.0
C4A A:HEM501 3.1 55.0 1.0
C1B A:HEM501 3.1 53.0 1.0
C4B A:HEM501 3.1 56.3 1.0
CB A:CYS184 3.3 41.5 1.0
CHD A:HEM501 3.4 67.1 1.0
CHA A:HEM501 3.5 59.3 1.0
CHC A:HEM501 3.5 57.6 1.0
CHB A:HEM501 3.5 56.3 1.0
C04 A:KMI503 3.9 39.2 1.0
CA A:CYS184 4.0 41.4 1.0
C03 A:KMI503 4.1 35.9 1.0
C07 A:KMI503 4.2 48.2 1.0
C05 A:KMI503 4.2 41.0 1.0
C2D A:HEM501 4.3 56.6 1.0
C3D A:HEM501 4.3 61.2 1.0
C3C A:HEM501 4.3 65.1 1.0
C2C A:HEM501 4.3 57.5 1.0
C2B A:HEM501 4.3 47.6 1.0
C3A A:HEM501 4.3 59.0 1.0
C3B A:HEM501 4.3 49.3 1.0
C2A A:HEM501 4.3 61.2 1.0
NE1 A:TRP178 4.4 58.1 1.0
C02 A:KMI503 4.5 43.2 1.0
C06 A:KMI503 4.6 45.5 1.0
N01 A:KMI503 4.8 39.6 1.0
C A:CYS184 4.8 43.8 1.0
N A:VAL185 4.9 49.2 1.0
N A:GLY186 4.9 34.4 1.0
CD1 A:TRP178 4.9 52.9 1.0

Iron binding site 2 out of 4 in 7tsi

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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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:34.9
occ:1.00
 FE B:HEM501 0.0 34.9 1.0
NB B:HEM501 2.0 41.2 1.0
NA B:HEM501 2.0 38.2 1.0
NC B:HEM501 2.1 28.0 1.0
ND B:HEM501 2.1 33.2 1.0
SG B:CYS184 2.3 28.9 1.0
C4B B:HEM501 3.0 30.0 1.0
C4A B:HEM501 3.0 39.7 1.0
C1B B:HEM501 3.0 32.5 1.0
C1A B:HEM501 3.1 36.1 1.0
C1C B:HEM501 3.1 32.0 1.0
C1D B:HEM501 3.1 35.1 1.0
C4D B:HEM501 3.1 40.0 1.0
C4C B:HEM501 3.2 25.1 1.0
CB B:CYS184 3.3 21.9 1.0
CHB B:HEM501 3.4 31.5 1.0
CHC B:HEM501 3.4 24.2 1.0
CHA B:HEM501 3.5 32.8 1.0
CHD B:HEM501 3.5 29.3 1.0
C04 B:KMI503 3.9 25.7 1.0
C03 B:KMI503 4.0 22.5 1.0
CA B:CYS184 4.0 27.6 1.0
C05 B:KMI503 4.2 29.6 1.0
C3B B:HEM501 4.2 33.7 1.0
C2B B:HEM501 4.2 29.8 1.0
C3A B:HEM501 4.3 37.2 1.0
C07 B:KMI503 4.3 30.4 1.0
C2A B:HEM501 4.3 37.5 1.0
C2D B:HEM501 4.3 26.2 1.0
C2C B:HEM501 4.3 28.7 1.0
C3D B:HEM501 4.3 35.4 1.0
C02 B:KMI503 4.4 26.7 1.0
NE1 B:TRP178 4.4 42.1 1.0
C3C B:HEM501 4.4 28.1 1.0
C06 B:KMI503 4.6 33.5 1.0
N01 B:KMI503 4.6 28.0 1.0
N B:GLY186 4.8 41.3 1.0
C B:CYS184 4.8 25.9 1.0
CD1 B:TRP178 5.0 23.9 1.0

Iron binding site 3 out of 4 in 7tsi

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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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:42.3
occ:1.00
 FE C:HEM501 0.0 42.3 1.0
ND C:HEM501 2.1 42.5 1.0
NB C:HEM501 2.1 41.0 1.0
NA C:HEM501 2.1 49.4 1.0
NC C:HEM501 2.1 45.4 1.0
SG C:CYS184 2.3 48.3 1.0
C1B C:HEM501 3.1 45.3 1.0
C4B C:HEM501 3.1 38.2 1.0
C4D C:HEM501 3.1 46.2 1.0
C1D C:HEM501 3.1 43.2 1.0
C4A C:HEM501 3.1 46.9 1.0
C1A C:HEM501 3.1 46.8 1.0
C1C C:HEM501 3.1 44.8 1.0
C4C C:HEM501 3.1 50.2 1.0
CB C:CYS184 3.4 46.9 1.0
CHB C:HEM501 3.4 42.9 1.0
CHC C:HEM501 3.4 34.4 1.0
CHA C:HEM501 3.5 41.9 1.0
CHD C:HEM501 3.5 48.7 1.0
C04 C:KMI503 3.9 38.7 1.0
C03 C:KMI503 4.0 46.9 1.0
CA C:CYS184 4.0 43.4 1.0
C07 C:KMI503 4.2 35.8 1.0
C2B C:HEM501 4.3 37.4 1.0
C3B C:HEM501 4.3 46.8 1.0
C2D C:HEM501 4.3 41.3 1.0
C05 C:KMI503 4.3 41.3 1.0
C3D C:HEM501 4.3 37.3 1.0
C3A C:HEM501 4.3 45.5 1.0
C2A C:HEM501 4.3 54.4 1.0
C2C C:HEM501 4.4 56.1 1.0
C3C C:HEM501 4.4 50.4 1.0
NE1 C:TRP178 4.4 48.7 1.0
C02 C:KMI503 4.5 50.9 1.0
C06 C:KMI503 4.7 46.2 1.0
N C:GLY186 4.8 37.2 1.0
C C:CYS184 4.8 33.1 1.0
N01 C:KMI503 4.8 50.9 1.0
CD1 C:TRP178 4.9 41.3 1.0
N C:VAL185 4.9 41.5 1.0

Iron binding site 4 out of 4 in 7tsi

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Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-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 4-Methyl-6-(3-((Methylamino)Methyl)Phenyl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:34.2
occ:1.00
 FE D:HEM501 0.0 34.2 1.0
NA D:HEM501 2.0 32.0 1.0
NC D:HEM501 2.0 37.7 1.0
ND D:HEM501 2.1 38.2 1.0
NB D:HEM501 2.1 31.1 1.0
SG D:CYS184 2.3 32.0 1.0
C4A D:HEM501 3.0 30.5 1.0
C4C D:HEM501 3.0 27.4 1.0
C1D D:HEM501 3.1 34.9 1.0
C1B D:HEM501 3.1 40.0 1.0
C1A D:HEM501 3.1 25.9 1.0
C1C D:HEM501 3.1 29.7 1.0
C4D D:HEM501 3.1 40.3 1.0
C4B D:HEM501 3.2 31.6 1.0
CB D:CYS184 3.3 33.9 1.0
CHD D:HEM501 3.4 42.9 1.0
CHB D:HEM501 3.4 35.4 1.0
CHA D:HEM501 3.5 26.6 1.0
CHC D:HEM501 3.5 36.5 1.0
C04 D:KMI503 3.9 27.6 1.0
C03 D:KMI503 4.0 20.5 1.0
CA D:CYS184 4.1 21.7 1.0
C07 D:KMI503 4.2 17.0 1.0
C3A D:HEM501 4.2 35.2 1.0
C05 D:KMI503 4.2 30.1 1.0
C2A D:HEM501 4.3 36.1 1.0
C3C D:HEM501 4.3 36.2 1.0
C2D D:HEM501 4.3 42.1 1.0
C2C D:HEM501 4.3 33.4 1.0
C2B D:HEM501 4.3 25.9 1.0
C3D D:HEM501 4.3 44.8 1.0
C3B D:HEM501 4.4 36.6 1.0
NE1 D:TRP178 4.4 41.3 1.0
C02 D:KMI503 4.4 30.5 1.0
C06 D:KMI503 4.7 33.0 1.0
N01 D:KMI503 4.8 32.3 1.0
C D:CYS184 4.8 29.1 1.0
N D:VAL185 4.8 27.4 1.0
N D:GLY186 4.8 23.8 1.0
CD1 D:TRP178 4.9 38.0 1.0

Reference:

D.Vasu, H.Li, C.D.Hardy, T.L.Poulos, R.B.Silverman. 2-Aminopyridines with A Shortened Amino Sidechain As Potent, Selective, and Highly Permeable Human Neuronal Nitric Oxide Synthase Inhibitors. Bioorg.Med.Chem. V. 69 16878 2022.
ISSN: ESSN 1464-3391
PubMed: 35772285
DOI: 10.1016/J.BMC.2022.116878
Page generated: Fri Aug 9 02:28:02 2024

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