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Iron in PDB 5uo8: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile, PDB code: 5uo8 was solved by G.Chreifi, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.54 / 2.18
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.370, 152.740, 108.511, 90.00, 90.74, 90.00
R / Rfree (%) 20.6 / 27.2

Other elements in 5uo8:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile also contains other interesting chemical elements:

Gadolinium (Gd) 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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile (pdb code 5uo8). 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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile, PDB code: 5uo8:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5uo8

Go back to Iron Binding Sites List in 5uo8
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile


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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:40.2
occ:1.00
 FE A:HEM501 0.0 40.2 1.0
NA A:HEM501 2.0 43.2 1.0
ND A:HEM501 2.1 41.5 1.0
NB A:HEM501 2.1 38.6 1.0
NC A:HEM501 2.1 53.2 1.0
SG A:CYS184 2.3 33.8 1.0
C1A A:HEM501 3.0 37.7 1.0
C4A A:HEM501 3.0 41.6 1.0
C4D A:HEM501 3.1 41.3 1.0
C1B A:HEM501 3.1 36.8 1.0
C1D A:HEM501 3.1 51.1 1.0
C1C A:HEM501 3.1 55.2 1.0
C4C A:HEM501 3.1 51.1 1.0
C4B A:HEM501 3.2 44.8 1.0
CB A:CYS184 3.3 28.4 1.0
C04 A:8EV503 3.3 49.6 1.0
CHA A:HEM501 3.4 37.8 1.0
CHB A:HEM501 3.4 42.0 1.0
CHD A:HEM501 3.5 53.8 1.0
CHC A:HEM501 3.5 51.1 1.0
C05 A:8EV503 3.6 52.7 1.0
C06 A:8EV503 3.8 56.0 1.0
C03 A:8EV503 3.9 49.3 1.0
CA A:CYS184 4.1 31.0 1.0
C2A A:HEM501 4.2 43.6 1.0
C3A A:HEM501 4.3 40.0 1.0
C3D A:HEM501 4.3 45.5 1.0
C2D A:HEM501 4.3 43.6 1.0
C10 A:8EV503 4.3 48.0 1.0
C2B A:HEM501 4.3 37.8 1.0
C3C A:HEM501 4.4 51.9 1.0
C2C A:HEM501 4.4 53.9 1.0
C3B A:HEM501 4.4 40.9 1.0
NE1 A:TRP178 4.5 38.7 1.0
C02 A:8EV503 4.6 49.3 1.0
C07 A:8EV503 4.7 53.5 1.0
N01 A:8EV503 4.8 48.2 1.0
C A:CYS184 4.8 34.2 1.0
N A:GLY186 4.9 29.2 1.0

Iron binding site 2 out of 4 in 5uo8

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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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile


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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:29.1
occ:1.00
 FE B:HEM501 0.0 29.1 1.0
NA B:HEM501 2.1 33.2 1.0
ND B:HEM501 2.1 25.8 1.0
NB B:HEM501 2.1 28.2 1.0
NC B:HEM501 2.2 33.9 1.0
SG B:CYS184 2.2 23.3 1.0
C1A B:HEM501 3.1 24.8 1.0
C4D B:HEM501 3.1 36.2 1.0
C4A B:HEM501 3.1 32.4 1.0
C1B B:HEM501 3.1 32.2 1.0
C1D B:HEM501 3.1 31.4 1.0
C4B B:HEM501 3.1 38.7 1.0
C1C B:HEM501 3.2 38.6 1.0
C4C B:HEM501 3.2 33.7 1.0
CB B:CYS184 3.4 39.4 1.0
CHA B:HEM501 3.4 24.9 1.0
C04 B:8EV503 3.4 39.9 1.0
CHB B:HEM501 3.5 21.8 1.0
CHD B:HEM501 3.5 34.4 1.0
CHC B:HEM501 3.5 37.6 1.0
C05 B:8EV503 3.6 38.5 1.0
C06 B:8EV503 3.8 31.0 1.0
C03 B:8EV503 4.0 40.8 1.0
CA B:CYS184 4.1 31.6 1.0
NE1 B:TRP178 4.3 40.1 1.0
C2A B:HEM501 4.3 32.0 1.0
C3A B:HEM501 4.3 36.5 1.0
C3D B:HEM501 4.3 28.5 1.0
C10 B:8EV503 4.3 44.5 1.0
C2D B:HEM501 4.3 30.3 1.0
C2B B:HEM501 4.3 34.6 1.0
C3B B:HEM501 4.3 35.2 1.0
C2C B:HEM501 4.4 37.4 1.0
C3C B:HEM501 4.4 40.4 1.0
C07 B:8EV503 4.7 39.7 1.0
C02 B:8EV503 4.7 32.1 1.0
N B:GLY186 4.7 25.8 1.0
N01 B:8EV503 4.8 35.8 1.0
C B:CYS184 4.8 30.6 1.0
N B:VAL185 4.9 37.2 1.0
CD1 B:TRP178 4.9 34.5 1.0

Iron binding site 3 out of 4 in 5uo8

Go back to Iron Binding Sites List in 5uo8
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile


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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:33.2
occ:1.00
 FE C:HEM501 0.0 33.2 1.0
NA C:HEM501 2.0 38.2 1.0
ND C:HEM501 2.0 38.8 1.0
NC C:HEM501 2.1 50.0 1.0
NB C:HEM501 2.2 44.5 1.0
SG C:CYS184 2.3 30.6 1.0
C4D C:HEM501 3.0 39.9 1.0
C1A C:HEM501 3.0 31.2 1.0
C1D C:HEM501 3.1 38.2 1.0
C4A C:HEM501 3.1 39.5 1.0
C4C C:HEM501 3.2 49.6 1.0
C1C C:HEM501 3.2 55.9 1.0
C1B C:HEM501 3.2 42.8 1.0
C4B C:HEM501 3.2 51.5 1.0
CHA C:HEM501 3.3 31.2 1.0
CB C:CYS184 3.3 24.9 1.0
CHD C:HEM501 3.5 42.5 1.0
CHB C:HEM501 3.5 39.4 1.0
CHC C:HEM501 3.5 55.5 1.0
C04 C:8EV503 3.6 39.4 1.0
C05 C:8EV503 3.8 44.5 1.0
C03 C:8EV503 4.0 45.8 1.0
CA C:CYS184 4.0 28.1 1.0
C06 C:8EV503 4.1 43.8 1.0
C3D C:HEM501 4.2 41.0 1.0
C2A C:HEM501 4.3 41.4 1.0
C2D C:HEM501 4.3 35.0 1.0
C3A C:HEM501 4.3 38.5 1.0
C10 C:8EV503 4.3 40.8 1.0
NE1 C:TRP178 4.3 43.5 1.0
C3C C:HEM501 4.4 56.4 1.0
C2C C:HEM501 4.4 54.9 1.0
C2B C:HEM501 4.4 44.8 1.0
C3B C:HEM501 4.4 50.5 1.0
C02 C:8EV503 4.5 46.3 1.0
N01 C:8EV503 4.6 45.5 1.0
C C:CYS184 4.8 25.8 1.0
N C:GLY186 4.9 27.3 1.0
C07 C:8EV503 4.9 48.0 1.0
N C:VAL185 4.9 23.0 1.0
CD1 C:TRP178 5.0 43.9 1.0

Iron binding site 4 out of 4 in 5uo8

Go back to Iron Binding Sites List in 5uo8
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile


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 3-[(2-Aminoquinolin-7-Yl)Methoxy]-5-((Methylamino) Methyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:29.2
occ:1.00
 FE D:HEM501 0.0 29.2 1.0
NA D:HEM501 2.0 29.8 1.0
NB D:HEM501 2.1 37.2 1.0
NC D:HEM501 2.1 26.9 1.0
ND D:HEM501 2.2 28.7 1.0
SG D:CYS184 2.2 21.2 1.0
C4A D:HEM501 3.0 38.7 1.0
C1A D:HEM501 3.1 32.7 1.0
C1B D:HEM501 3.1 41.9 1.0
C4C D:HEM501 3.1 38.9 1.0
C1D D:HEM501 3.1 32.4 1.0
C4D D:HEM501 3.2 38.2 1.0
C4B D:HEM501 3.2 35.6 1.0
C1C D:HEM501 3.2 30.0 1.0
CHB D:HEM501 3.4 39.2 1.0
CHD D:HEM501 3.4 32.2 1.0
CB D:CYS184 3.5 23.6 1.0
CHA D:HEM501 3.5 26.4 1.0
CHC D:HEM501 3.5 23.4 1.0
C04 D:8EV503 3.7 23.4 1.0
C05 D:8EV503 3.8 28.9 1.0
C06 D:8EV503 4.1 26.1 1.0
CA D:CYS184 4.1 27.8 1.0
C03 D:8EV503 4.2 30.0 1.0
C3A D:HEM501 4.3 42.9 1.0
C2A D:HEM501 4.3 40.5 1.0
C2B D:HEM501 4.3 37.4 1.0
C10 D:8EV503 4.3 31.5 1.0
C3B D:HEM501 4.4 37.6 1.0
C2D D:HEM501 4.4 35.2 1.0
C3C D:HEM501 4.4 41.8 1.0
C3D D:HEM501 4.4 38.3 1.0
C2C D:HEM501 4.4 31.8 1.0
NE1 D:TRP178 4.5 39.0 1.0
C02 D:8EV503 4.7 21.6 1.0
N01 D:8EV503 4.7 18.3 1.0
N D:VAL185 4.8 23.9 1.0
N D:GLY186 4.8 28.7 1.0
C07 D:8EV503 4.8 33.5 1.0
C D:CYS184 4.9 23.6 1.0

Reference:

M.A.Cinelli, H.Li, G.Chreifi, T.L.Poulos, R.B.Silverman. Nitrile in the Hole: Discovery of A Small Auxiliary Pocket in Neuronal Nitric Oxide Synthase Leading to the Development of Potent and Selective 2-Aminoquinoline Inhibitors. J. Med. Chem. V. 60 3958 2017.
ISSN: ISSN 1520-4804
PubMed: 28422508
DOI: 10.1021/ACS.JMEDCHEM.7B00259
Page generated: Tue Aug 6 09:58:35 2024

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