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

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-(Methylamino)Propyl)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)Propyl)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)Propyl)Pyridin-2-Amine, PDB code: 7tsh 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) 39.11 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.798, 152.74, 108.589, 90, 90.72, 90
R / Rfree (%) 21.4 / 27

Other elements in 7tsh:

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

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

Iron binding site 1 out of 4 in 7tsh

Go back to Iron Binding Sites List in 7tsh
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)Propyl)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)Propyl)Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:60.7
occ:1.00
 FE A:HEM501 0.0 60.7 1.0
ND A:HEM501 2.0 70.0 1.0
NC A:HEM501 2.1 81.6 1.0
NA A:HEM501 2.1 66.9 1.0
NB A:HEM501 2.1 68.2 1.0
SG A:CYS184 2.3 48.0 1.0
C4C A:HEM501 3.0 88.0 1.0
C1D A:HEM501 3.0 79.0 1.0
C4D A:HEM501 3.1 72.4 1.0
C1C A:HEM501 3.1 82.6 1.0
C4A A:HEM501 3.1 66.3 1.0
C1A A:HEM501 3.1 61.8 1.0
C1B A:HEM501 3.1 69.0 1.0
C4B A:HEM501 3.1 69.7 1.0
CB A:CYS184 3.3 43.7 1.0
CHD A:HEM501 3.4 88.4 1.0
CHA A:HEM501 3.5 67.3 1.0
CHB A:HEM501 3.5 68.8 1.0
CHC A:HEM501 3.5 75.7 1.0
C03 A:KKU503 3.9 48.7 1.0
C04 A:KKU503 4.0 54.4 1.0
CA A:CYS184 4.0 49.0 1.0
C07 A:KKU503 4.2 52.2 1.0
C3C A:HEM501 4.3 88.7 1.0
C2D A:HEM501 4.3 75.8 1.0
C2C A:HEM501 4.3 83.4 1.0
C3D A:HEM501 4.3 73.7 1.0
C3A A:HEM501 4.3 63.7 1.0
C2A A:HEM501 4.3 57.3 1.0
C2B A:HEM501 4.3 66.7 1.0
C3B A:HEM501 4.4 63.8 1.0
C02 A:KKU503 4.4 51.7 1.0
C05 A:KKU503 4.4 54.7 1.0
NE1 A:TRP178 4.6 73.1 1.0
N01 A:KKU503 4.8 50.8 1.0
C06 A:KKU503 4.8 49.3 1.0
C A:CYS184 4.9 56.4 1.0
N02 A:KKU503 5.0 52.6 1.0

Iron binding site 2 out of 4 in 7tsh

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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)Propyl)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)Propyl)Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:36.0
occ:1.00
 FE B:HEM501 0.0 36.0 1.0
NC B:HEM501 2.0 48.1 1.0
ND B:HEM501 2.1 40.1 1.0
NB B:HEM501 2.1 45.7 1.0
NA B:HEM501 2.2 44.6 1.0
SG B:CYS184 2.3 31.7 1.0
C4C B:HEM501 3.0 50.6 1.0
C1C B:HEM501 3.1 49.6 1.0
C1D B:HEM501 3.1 46.0 1.0
C4D B:HEM501 3.1 44.2 1.0
C4B B:HEM501 3.1 46.0 1.0
C1B B:HEM501 3.1 44.0 1.0
C4A B:HEM501 3.2 45.4 1.0
C1A B:HEM501 3.2 42.8 1.0
CB B:CYS184 3.3 38.1 1.0
CHD B:HEM501 3.4 47.6 1.0
CHC B:HEM501 3.4 51.1 1.0
CHB B:HEM501 3.5 34.4 1.0
CHA B:HEM501 3.5 37.2 1.0
CA B:CYS184 4.0 42.9 1.0
C03 B:KKU503 4.1 36.3 1.0
C04 B:KKU503 4.2 48.6 1.0
C3C B:HEM501 4.2 48.8 1.0
C2C B:HEM501 4.3 48.6 1.0
C3D B:HEM501 4.3 42.3 1.0
C2D B:HEM501 4.3 39.1 1.0
NE1 B:TRP178 4.3 46.1 1.0
C2B B:HEM501 4.4 44.7 1.0
C3B B:HEM501 4.4 44.9 1.0
C2A B:HEM501 4.4 43.8 1.0
C3A B:HEM501 4.4 43.9 1.0
C07 B:KKU503 4.5 51.0 1.0
C02 B:KKU503 4.5 40.0 1.0
C05 B:KKU503 4.7 47.1 1.0
C B:CYS184 4.8 32.8 1.0
N B:GLY186 4.8 37.4 1.0
N B:VAL185 4.9 29.3 1.0
N01 B:KKU503 5.0 42.6 1.0

Iron binding site 3 out of 4 in 7tsh

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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)Propyl)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)Propyl)Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:46.0
occ:1.00
 FE C:HEM501 0.0 46.0 1.0
NC C:HEM501 2.1 53.3 1.0
ND C:HEM501 2.1 56.3 1.0
NA C:HEM501 2.1 51.5 1.0
NB C:HEM501 2.1 53.4 1.0
SG C:CYS184 2.3 42.9 1.0
C4C C:HEM501 3.1 58.2 1.0
C1D C:HEM501 3.1 56.8 1.0
C1C C:HEM501 3.1 55.6 1.0
C4D C:HEM501 3.1 54.2 1.0
C4A C:HEM501 3.1 51.2 1.0
C1B C:HEM501 3.1 54.3 1.0
C4B C:HEM501 3.1 51.9 1.0
C1A C:HEM501 3.1 47.3 1.0
CB C:CYS184 3.3 45.7 1.0
CHD C:HEM501 3.4 57.3 1.0
CHB C:HEM501 3.4 53.6 1.0
CHC C:HEM501 3.4 49.4 1.0
CHA C:HEM501 3.5 45.5 1.0
C03 C:KKU503 4.0 52.0 1.0
CA C:CYS184 4.1 43.1 1.0
C04 C:KKU503 4.2 42.4 1.0
C3C C:HEM501 4.3 61.8 1.0
C2C C:HEM501 4.3 61.6 1.0
C2D C:HEM501 4.3 46.9 1.0
C3D C:HEM501 4.3 52.3 1.0
C3A C:HEM501 4.3 51.5 1.0
C02 C:KKU503 4.3 58.4 1.0
C2B C:HEM501 4.3 53.4 1.0
C3B C:HEM501 4.3 59.9 1.0
C2A C:HEM501 4.3 51.4 1.0
NE1 C:TRP178 4.5 51.6 1.0
C07 C:KKU503 4.7 45.1 1.0
C05 C:KKU503 4.7 52.4 1.0
N02 C:KKU503 4.8 52.5 1.0
N01 C:KKU503 4.8 63.1 1.0
C C:CYS184 4.8 43.3 1.0
N C:GLY186 4.8 46.2 1.0
N C:VAL185 4.9 42.8 1.0

Iron binding site 4 out of 4 in 7tsh

Go back to Iron Binding Sites List in 7tsh
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)Propyl)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)Propyl)Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:32.7
occ:1.00
 FE D:HEM501 0.0 32.7 1.0
ND D:HEM501 2.0 41.2 1.0
NA D:HEM501 2.1 42.6 1.0
NB D:HEM501 2.1 41.8 1.0
NC D:HEM501 2.1 41.0 1.0
SG D:CYS184 2.3 31.7 1.0
C1D D:HEM501 3.0 44.7 1.0
C4A D:HEM501 3.0 40.0 1.0
C1B D:HEM501 3.1 45.6 1.0
C4D D:HEM501 3.1 43.8 1.0
C4C D:HEM501 3.1 41.5 1.0
C1A D:HEM501 3.1 45.4 1.0
C4B D:HEM501 3.2 39.1 1.0
C1C D:HEM501 3.2 44.3 1.0
CB D:CYS184 3.2 41.0 1.0
CHB D:HEM501 3.3 33.8 1.0
CHD D:HEM501 3.4 40.8 1.0
CHA D:HEM501 3.5 43.7 1.0
CHC D:HEM501 3.6 45.0 1.0
CA D:CYS184 4.1 36.4 1.0
C03 D:KKU503 4.1 44.0 1.0
C04 D:KKU503 4.2 50.2 1.0
C2D D:HEM501 4.3 44.5 1.0
C3A D:HEM501 4.3 47.2 1.0
C3D D:HEM501 4.3 40.7 1.0
C2A D:HEM501 4.3 47.3 1.0
C2B D:HEM501 4.3 41.3 1.0
C3C D:HEM501 4.4 44.9 1.0
C3B D:HEM501 4.4 40.6 1.0
C2C D:HEM501 4.4 41.9 1.0
C07 D:KKU503 4.5 42.0 1.0
NE1 D:TRP178 4.5 45.5 1.0
C02 D:KKU503 4.5 42.2 1.0
C05 D:KKU503 4.6 49.2 1.0
C D:CYS184 4.8 35.2 1.0
N D:GLY186 4.8 34.1 1.0
N01 D:KKU503 5.0 32.7 1.0
N D:VAL185 5.0 35.7 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 02:27:52 2024

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