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Iron in PDB 8fgr: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine, PDB code: 8fgr 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) 48.60 / 1.98
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.783, 150.897, 107.428, 90, 90.6, 90
R / Rfree (%) 20.8 / 26.3

Other elements in 8fgr:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine also contains other interesting chemical elements:

Chlorine (Cl) 4 atoms
Zinc (Zn) 2 atoms
Fluorine (F) 8 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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine (pdb code 8fgr). 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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine, PDB code: 8fgr:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8fgr

Go back to Iron Binding Sites List in 8fgr
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:50.3
occ:1.00
 FE A:HEM501 0.0 50.3 1.0
ND A:HEM501 2.0 53.5 1.0
NC A:HEM501 2.1 61.2 1.0
NA A:HEM501 2.1 51.7 1.0
NB A:HEM501 2.1 47.0 1.0
SG A:CYS184 2.3 43.0 1.0
C4D A:HEM501 3.0 59.1 1.0
C1D A:HEM501 3.0 61.3 1.0
C4C A:HEM501 3.1 65.0 1.0
C1A A:HEM501 3.1 54.7 1.0
C4A A:HEM501 3.1 49.7 1.0
C1B A:HEM501 3.1 55.3 1.0
C1C A:HEM501 3.1 58.9 1.0
C4B A:HEM501 3.1 52.6 1.0
CB A:CYS184 3.2 39.8 1.0
CHA A:HEM501 3.4 54.0 1.0
CHD A:HEM501 3.4 62.9 1.0
CHB A:HEM501 3.5 53.5 1.0
CHC A:HEM501 3.5 54.6 1.0
C04 A:XVZ511 3.9 53.2 1.0
CA A:CYS184 4.0 41.6 1.0
C03 A:XVZ511 4.1 45.9 1.0
C05 A:XVZ511 4.1 55.9 1.0
C3D A:HEM501 4.2 65.0 1.0
C2D A:HEM501 4.2 63.8 1.0
C07 A:XVZ511 4.3 56.5 1.0
C2B A:HEM501 4.3 48.3 1.0
C3C A:HEM501 4.3 65.3 1.0
C3A A:HEM501 4.3 53.9 1.0
C2A A:HEM501 4.3 55.7 1.0
C2C A:HEM501 4.3 61.1 1.0
C3B A:HEM501 4.4 50.8 1.0
NE1 A:TRP178 4.4 54.6 1.0
C02 A:XVZ511 4.4 43.8 1.0
C06 A:XVZ511 4.5 55.9 1.0
N01 A:XVZ511 4.6 48.5 1.0
C A:CYS184 4.8 40.2 1.0
N A:GLY186 4.9 47.4 1.0
N A:VAL185 4.9 45.1 1.0
CD1 A:TRP178 5.0 48.1 1.0

Iron binding site 2 out of 4 in 8fgr

Go back to Iron Binding Sites List in 8fgr
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:32.9
occ:1.00
 FE B:HEM502 0.0 32.9 1.0
ND B:HEM502 2.0 36.8 1.0
NC B:HEM502 2.1 27.5 1.0
NB B:HEM502 2.1 39.0 1.0
NA B:HEM502 2.1 36.1 1.0
SG B:CYS184 2.4 26.0 1.0
C1D B:HEM502 3.0 33.9 1.0
C4D B:HEM502 3.0 38.8 1.0
C4C B:HEM502 3.1 29.2 1.0
C4B B:HEM502 3.1 32.1 1.0
C1C B:HEM502 3.1 33.9 1.0
C1B B:HEM502 3.1 34.1 1.0
C1A B:HEM502 3.1 30.7 1.0
C4A B:HEM502 3.2 32.5 1.0
CB B:CYS184 3.2 24.6 1.0
CHD B:HEM502 3.4 28.0 1.0
CHC B:HEM502 3.5 29.1 1.0
CHA B:HEM502 3.5 35.2 1.0
CHB B:HEM502 3.5 31.1 1.0
CA B:CYS184 3.9 32.2 1.0
C04 B:XVZ501 4.0 36.0 1.0
C03 B:XVZ501 4.1 23.6 1.0
C2D B:HEM502 4.2 30.7 1.0
NE1 B:TRP178 4.2 38.7 1.0
C3D B:HEM502 4.2 29.4 1.0
C05 B:XVZ501 4.3 32.9 1.0
C3B B:HEM502 4.3 31.4 1.0
C2B B:HEM502 4.3 31.4 1.0
C3C B:HEM502 4.3 31.3 1.0
C2C B:HEM502 4.3 29.4 1.0
C2A B:HEM502 4.4 38.9 1.0
C3A B:HEM502 4.4 35.8 1.0
C07 B:XVZ501 4.4 31.7 1.0
C02 B:XVZ501 4.4 32.1 1.0
C06 B:XVZ501 4.6 37.7 1.0
N01 B:XVZ501 4.7 32.6 1.0
C B:CYS184 4.7 29.9 1.0
N B:GLY186 4.8 37.1 1.0
CD1 B:TRP178 4.9 26.0 1.0
N B:VAL185 4.9 29.0 1.0

Iron binding site 3 out of 4 in 8fgr

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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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:41.5
occ:1.00
 FE C:HEM501 0.0 41.5 1.0
NB C:HEM501 2.0 37.6 1.0
ND C:HEM501 2.1 42.3 1.0
NA C:HEM501 2.1 45.0 1.0
NC C:HEM501 2.1 50.0 1.0
SG C:CYS184 2.3 41.9 1.0
C4B C:HEM501 3.0 44.0 1.0
C1B C:HEM501 3.0 45.4 1.0
C1C C:HEM501 3.1 54.5 1.0
C4D C:HEM501 3.1 47.5 1.0
C4A C:HEM501 3.1 35.0 1.0
C1A C:HEM501 3.1 47.8 1.0
C1D C:HEM501 3.1 48.2 1.0
C4C C:HEM501 3.2 51.2 1.0
CB C:CYS184 3.3 44.5 1.0
CHC C:HEM501 3.4 48.2 1.0
CHB C:HEM501 3.4 39.3 1.0
CHA C:HEM501 3.4 41.3 1.0
CHD C:HEM501 3.5 45.8 1.0
C04 C:XVZ503 3.9 42.3 1.0
C03 C:XVZ503 4.0 49.4 1.0
CA C:CYS184 4.0 45.6 1.0
C05 C:XVZ503 4.2 47.1 1.0
C3B C:HEM501 4.2 43.2 1.0
C2B C:HEM501 4.3 40.6 1.0
C3A C:HEM501 4.3 44.0 1.0
C3D C:HEM501 4.3 48.8 1.0
C2C C:HEM501 4.3 60.2 1.0
C2A C:HEM501 4.3 49.4 1.0
C07 C:XVZ503 4.3 37.2 1.0
C2D C:HEM501 4.3 46.2 1.0
C02 C:XVZ503 4.3 50.8 1.0
C3C C:HEM501 4.4 51.2 1.0
NE1 C:TRP178 4.4 46.8 1.0
C06 C:XVZ503 4.6 51.5 1.0
N01 C:XVZ503 4.6 52.8 1.0
N C:GLY186 4.8 36.2 1.0
C C:CYS184 4.8 32.3 1.0
N C:VAL185 5.0 38.9 1.0
CD1 C:TRP178 5.0 44.7 1.0

Iron binding site 4 out of 4 in 8fgr

Go back to Iron Binding Sites List in 8fgr
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-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 6-(5-(2-Aminoethyl)-2,3-Difluorophenethyl)-4- Methylpyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:31.9
occ:1.00
 FE D:HEM501 0.0 31.9 1.0
ND D:HEM501 2.0 40.9 1.0
NA D:HEM501 2.1 23.2 1.0
NB D:HEM501 2.1 33.6 1.0
NC D:HEM501 2.1 26.2 1.0
SG D:CYS184 2.2 30.1 1.0
C1D D:HEM501 3.0 36.1 1.0
C4D D:HEM501 3.0 41.1 1.0
C1A D:HEM501 3.1 30.9 1.0
C4A D:HEM501 3.1 29.4 1.0
C1B D:HEM501 3.1 32.2 1.0
C4B D:HEM501 3.1 28.1 1.0
C4C D:HEM501 3.1 28.6 1.0
C1C D:HEM501 3.1 31.0 1.0
CB D:CYS184 3.3 38.8 1.0
CHD D:HEM501 3.4 29.4 1.0
CHA D:HEM501 3.4 27.7 1.0
CHB D:HEM501 3.4 31.0 1.0
CHC D:HEM501 3.5 26.8 1.0
C04 D:XVZ503 3.8 31.9 1.0
C03 D:XVZ503 3.9 28.6 1.0
CA D:CYS184 4.0 33.7 1.0
C05 D:XVZ503 4.0 31.9 1.0
C07 D:XVZ503 4.1 18.6 1.0
C2D D:HEM501 4.2 39.2 1.0
C3D D:HEM501 4.2 42.2 1.0
C2A D:HEM501 4.3 34.2 1.0
C3A D:HEM501 4.3 32.6 1.0
C2B D:HEM501 4.3 31.3 1.0
C3B D:HEM501 4.3 29.6 1.0
C02 D:XVZ503 4.3 30.3 1.0
C3C D:HEM501 4.4 31.9 1.0
C2C D:HEM501 4.4 30.1 1.0
C06 D:XVZ503 4.4 39.1 1.0
NE1 D:TRP178 4.5 30.8 1.0
N01 D:XVZ503 4.6 33.2 1.0
C D:CYS184 4.7 32.1 1.0
N D:GLY186 4.7 24.6 1.0
N D:VAL185 4.9 27.8 1.0

Reference:

D.Vasu, H.T.Do, H.Li, C.D.Hardy, A.Awasthi, T.L.Poulos, R.B.Silverman. Potent, Selective, and Membrane Permeable 2-Amino-4-Substituted Pyridine-Based Neuronal Nitric Oxide Synthase Inhibitors. J.Med.Chem. V. 66 9934 2023.
ISSN: ISSN 0022-2623
PubMed: 37433128
DOI: 10.1021/ACS.JMEDCHEM.3C00782
Page generated: Sat Aug 10 03:52:18 2024

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