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Iron in PDB 7tsk: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-(Methylamino)Prop-1-Yn-1-Yl)Pyridin-2- Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-(Methylamino)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)Pyridin-2- Amine, PDB code: 7tsk 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) 36.40 / 2.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.745, 154.022, 109.19, 90, 90.49, 90
R / Rfree (%) 20.7 / 26.4

Other elements in 7tsk:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-6-(3-(Methylamino)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)Pyridin-2- Amine (pdb code 7tsk). 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)Prop-1-Yn-1-Yl)Pyridin-2- Amine, PDB code: 7tsk:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 7tsk

Go back to Iron Binding Sites List in 7tsk
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)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:45.3
occ:1.00
 FE A:HEM501 0.0 45.3 1.0
ND A:HEM501 2.1 58.2 1.0
NA A:HEM501 2.1 58.2 1.0
NC A:HEM501 2.1 63.4 1.0
NB A:HEM501 2.1 53.1 1.0
SG A:CYS184 2.4 43.2 1.0
C1B A:HEM501 3.1 58.5 1.0
C4C A:HEM501 3.1 64.5 1.0
C4A A:HEM501 3.1 58.8 1.0
C1D A:HEM501 3.1 62.8 1.0
C4D A:HEM501 3.1 58.9 1.0
C1A A:HEM501 3.1 56.6 1.0
C1C A:HEM501 3.1 64.5 1.0
C4B A:HEM501 3.1 54.0 1.0
CHB A:HEM501 3.4 53.4 1.0
CHD A:HEM501 3.4 65.3 1.0
CHA A:HEM501 3.5 57.2 1.0
CHC A:HEM501 3.5 63.9 1.0
CB A:CYS184 3.5 46.4 1.0
C03 A:K9C503 3.7 45.1 1.0
C04 A:K9C503 3.8 50.6 1.0
C07 A:K9C503 4.0 45.4 1.0
CA A:CYS184 4.2 41.9 1.0
C02 A:K9C503 4.3 48.8 1.0
C3A A:HEM501 4.3 56.8 1.0
C2B A:HEM501 4.3 56.8 1.0
C2A A:HEM501 4.3 55.5 1.0
C3D A:HEM501 4.3 63.4 1.0
C2D A:HEM501 4.3 59.9 1.0
C3C A:HEM501 4.3 62.4 1.0
C2C A:HEM501 4.3 63.1 1.0
C3B A:HEM501 4.3 57.7 1.0
C05 A:K9C503 4.4 52.8 1.0
NE1 A:TRP178 4.5 64.1 1.0
N01 A:K9C503 4.8 48.3 1.0
C06 A:K9C503 4.8 47.1 1.0
N02 A:K9C503 4.8 48.1 1.0

Iron binding site 2 out of 4 in 7tsk

Go back to Iron Binding Sites List in 7tsk
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)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:32.2
occ:1.00
 FE B:HEM501 0.0 32.2 1.0
ND B:HEM501 2.1 40.0 1.0
NB B:HEM501 2.1 29.8 1.0
NC B:HEM501 2.1 29.3 1.0
NA B:HEM501 2.1 35.2 1.0
SG B:CYS184 2.3 28.3 1.0
C1D B:HEM501 3.1 33.8 1.0
C4C B:HEM501 3.1 41.5 1.0
C1B B:HEM501 3.1 42.4 1.0
C4D B:HEM501 3.1 43.0 1.0
C4B B:HEM501 3.1 35.0 1.0
C1C B:HEM501 3.1 34.9 1.0
C4A B:HEM501 3.1 38.0 1.0
C1A B:HEM501 3.2 37.5 1.0
CHD B:HEM501 3.4 37.3 1.0
CB B:CYS184 3.4 33.4 1.0
CHB B:HEM501 3.5 33.8 1.0
CHC B:HEM501 3.5 31.5 1.0
CHA B:HEM501 3.5 39.9 1.0
C03 B:K9C503 4.1 23.5 1.0
CA B:CYS184 4.1 28.9 1.0
C04 B:K9C503 4.2 33.8 1.0
C2B B:HEM501 4.3 33.0 1.0
C3B B:HEM501 4.3 31.4 1.0
C2D B:HEM501 4.3 33.4 1.0
C3D B:HEM501 4.3 38.2 1.0
NE1 B:TRP178 4.3 45.3 1.0
C3C B:HEM501 4.3 40.0 1.0
C2C B:HEM501 4.3 40.9 1.0
C3A B:HEM501 4.4 34.0 1.0
C2A B:HEM501 4.4 37.2 1.0
C07 B:K9C503 4.4 28.1 1.0
C02 B:K9C503 4.6 27.5 1.0
C05 B:K9C503 4.7 27.5 1.0
N B:GLY186 4.8 42.4 1.0
C B:CYS184 4.8 29.0 1.0
N B:VAL185 4.9 28.1 1.0
CD1 B:TRP178 5.0 34.2 1.0

Iron binding site 3 out of 4 in 7tsk

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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)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:40.4
occ:1.00
 FE C:HEM501 0.0 40.4 1.0
NC C:HEM501 2.0 56.5 1.0
ND C:HEM501 2.1 47.4 1.0
NB C:HEM501 2.1 46.1 1.0
NA C:HEM501 2.1 52.4 1.0
SG C:CYS184 2.3 38.9 1.0
C1C C:HEM501 3.0 49.5 1.0
C4C C:HEM501 3.0 52.5 1.0
C4B C:HEM501 3.1 49.5 1.0
C1D C:HEM501 3.1 48.1 1.0
C4D C:HEM501 3.1 54.5 1.0
C1B C:HEM501 3.1 48.7 1.0
C4A C:HEM501 3.1 43.8 1.0
C1A C:HEM501 3.2 49.4 1.0
CB C:CYS184 3.4 44.3 1.0
CHC C:HEM501 3.4 38.5 1.0
CHD C:HEM501 3.4 46.5 1.0
CHB C:HEM501 3.5 38.7 1.0
CHA C:HEM501 3.5 49.6 1.0
C03 C:K9C503 3.9 39.2 1.0
C04 C:K9C503 4.0 32.3 1.0
CA C:CYS184 4.1 42.0 1.0
C2C C:HEM501 4.2 55.3 1.0
C3C C:HEM501 4.2 49.8 1.0
C07 C:K9C503 4.3 42.9 1.0
C3B C:HEM501 4.3 56.8 1.0
C2D C:HEM501 4.3 42.9 1.0
C3D C:HEM501 4.3 48.6 1.0
C2B C:HEM501 4.3 49.7 1.0
C3A C:HEM501 4.4 44.8 1.0
C2A C:HEM501 4.4 50.7 1.0
C02 C:K9C503 4.4 41.9 1.0
NE1 C:TRP178 4.5 41.6 1.0
C05 C:K9C503 4.6 34.6 1.0
N C:GLY186 4.8 49.6 1.0
C C:CYS184 4.8 36.5 1.0
N C:VAL185 4.9 36.9 1.0
N01 C:K9C503 4.9 41.7 1.0
N02 C:K9C503 4.9 37.9 1.0
C06 C:K9C503 5.0 42.0 1.0

Iron binding site 4 out of 4 in 7tsk

Go back to Iron Binding Sites List in 7tsk
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)Prop-1-Yn-1-Yl)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)Prop-1-Yn-1-Yl)Pyridin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:28.2
occ:1.00
 FE D:HEM501 0.0 28.2 1.0
NA D:HEM501 2.1 31.8 1.0
ND D:HEM501 2.1 30.9 1.0
NB D:HEM501 2.1 26.9 1.0
NC D:HEM501 2.2 26.7 1.0
SG D:CYS184 2.3 26.9 1.0
C4A D:HEM501 3.0 29.8 1.0
C1D D:HEM501 3.1 35.1 1.0
C1B D:HEM501 3.1 27.8 1.0
C4D D:HEM501 3.1 36.7 1.0
C1A D:HEM501 3.1 32.4 1.0
C4C D:HEM501 3.1 24.9 1.0
C4B D:HEM501 3.2 24.9 1.0
C1C D:HEM501 3.2 24.7 1.0
CHB D:HEM501 3.4 28.8 1.0
CB D:CYS184 3.4 38.4 1.0
CHD D:HEM501 3.4 27.9 1.0
CHA D:HEM501 3.5 26.6 1.0
CHC D:HEM501 3.5 29.9 1.0
C03 D:K9C503 4.1 28.4 1.0
C04 D:K9C503 4.1 32.1 1.0
CA D:CYS184 4.1 30.3 1.0
C3A D:HEM501 4.3 27.3 1.0
C2D D:HEM501 4.3 34.2 1.0
C3D D:HEM501 4.3 38.6 1.0
C2A D:HEM501 4.3 36.3 1.0
C2B D:HEM501 4.3 29.5 1.0
C3B D:HEM501 4.4 30.1 1.0
C07 D:K9C503 4.4 23.3 1.0
C3C D:HEM501 4.4 24.5 1.0
C2C D:HEM501 4.4 26.7 1.0
NE1 D:TRP178 4.5 31.3 1.0
C02 D:K9C503 4.6 31.4 1.0
C05 D:K9C503 4.7 36.2 1.0
N D:GLY186 4.8 40.1 1.0
C D:CYS184 4.9 27.5 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 02:28:25 2024

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