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Iron in PDB 5uo9: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine, PDB code: 5uo9 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) 38.87 / 2.19
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.376, 152.087, 108.219, 90.00, 90.59, 90.00
R / Rfree (%) 21.2 / 27.6

Other elements in 5uo9:

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

Magnesium (Mg) 1 atom
Zinc (Zn) 2 atoms
Gadolinium (Gd) 4 atoms
Calcium (Ca) 1 atom
Chlorine (Cl) 5 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine (pdb code 5uo9). 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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine, PDB code: 5uo9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5uo9

Go back to Iron Binding Sites List in 5uo9
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:49.7
occ:1.00
 FE A:HEM501 0.0 49.7 1.0
NC A:HEM501 2.0 52.4 1.0
NB A:HEM501 2.1 54.8 1.0
ND A:HEM501 2.1 41.3 1.0
NA A:HEM501 2.1 52.7 1.0
SG A:CYS184 2.4 48.9 1.0
C1C A:HEM501 3.0 50.0 1.0
C4B A:HEM501 3.0 51.8 1.0
C4C A:HEM501 3.1 49.2 1.0
C1B A:HEM501 3.1 52.1 1.0
C4D A:HEM501 3.1 45.5 1.0
C1D A:HEM501 3.1 49.8 1.0
C1A A:HEM501 3.1 48.8 1.0
C4A A:HEM501 3.2 56.4 1.0
C04 A:8J4503 3.2 84.3 1.0
CB A:CYS184 3.2 53.8 1.0
CHC A:HEM501 3.4 49.8 1.0
CHA A:HEM501 3.5 46.6 1.0
CHD A:HEM501 3.5 50.5 1.0
CHB A:HEM501 3.5 56.8 1.0
C03 A:8J4503 3.5 80.7 1.0
C05 A:8J4503 3.9 88.5 1.0
CA A:CYS184 4.1 45.2 1.0
C3B A:HEM501 4.3 50.6 1.0
C2C A:HEM501 4.3 51.5 1.0
C2B A:HEM501 4.3 49.4 1.0
C3C A:HEM501 4.3 43.2 1.0
C06 A:8J4503 4.4 92.2 1.0
C3D A:HEM501 4.4 49.9 1.0
C2D A:HEM501 4.4 47.2 1.0
C2A A:HEM501 4.4 54.8 1.0
NE1 A:TRP178 4.4 64.3 1.0
C3A A:HEM501 4.4 53.0 1.0
C02 A:8J4503 4.5 82.1 1.0
C10 A:8J4503 4.8 87.6 1.0
C A:CYS184 4.8 43.4 1.0
N A:VAL185 4.9 43.7 1.0
CD1 A:TRP178 4.9 65.2 1.0
N01 A:8J4503 5.0 84.4 1.0

Iron binding site 2 out of 4 in 5uo9

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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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:34.4
occ:1.00
 FE B:HEM501 0.0 34.4 1.0
NA B:HEM501 2.1 43.4 1.0
ND B:HEM501 2.1 39.2 1.0
NB B:HEM501 2.1 40.6 1.0
NC B:HEM501 2.1 35.7 1.0
SG B:CYS184 2.3 28.0 1.0
C4D B:HEM501 3.1 42.3 1.0
C4A B:HEM501 3.1 40.3 1.0
C1B B:HEM501 3.1 39.0 1.0
C1A B:HEM501 3.1 36.9 1.0
C1D B:HEM501 3.1 36.5 1.0
C04 B:8J4503 3.1 62.3 1.0
C4C B:HEM501 3.1 36.1 1.0
C4B B:HEM501 3.2 41.3 1.0
C1C B:HEM501 3.2 35.8 1.0
CHB B:HEM501 3.4 37.1 1.0
CB B:CYS184 3.4 31.4 1.0
CHD B:HEM501 3.4 34.8 1.0
CHA B:HEM501 3.4 37.1 1.0
C03 B:8J4503 3.5 60.6 1.0
CHC B:HEM501 3.5 32.9 1.0
C05 B:8J4503 3.8 62.0 1.0
CA B:CYS184 4.1 35.3 1.0
C06 B:8J4503 4.2 63.4 1.0
C3A B:HEM501 4.3 34.0 1.0
C3D B:HEM501 4.3 40.8 1.0
C2A B:HEM501 4.3 32.6 1.0
C2B B:HEM501 4.3 42.2 1.0
C2D B:HEM501 4.3 33.9 1.0
NE1 B:TRP178 4.3 33.7 1.0
C3B B:HEM501 4.3 41.8 1.0
C3C B:HEM501 4.4 38.0 1.0
C2C B:HEM501 4.4 38.4 1.0
C02 B:8J4503 4.4 59.0 1.0
C10 B:8J4503 4.6 61.9 1.0
N B:GLY186 4.8 29.9 1.0
N B:VAL185 4.9 31.7 1.0
C B:CYS184 4.9 33.5 1.0
N01 B:8J4503 4.9 62.4 1.0
CD1 B:TRP178 5.0 31.5 1.0

Iron binding site 3 out of 4 in 5uo9

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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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:47.0
occ:1.00
 FE C:HEM501 0.0 47.0 1.0
NC C:HEM501 2.1 55.4 1.0
NA C:HEM501 2.1 51.1 1.0
ND C:HEM501 2.1 51.7 1.0
NB C:HEM501 2.1 54.6 1.0
SG C:CYS184 2.3 44.2 1.0
C1C C:HEM501 3.1 60.7 1.0
C4D C:HEM501 3.1 56.0 1.0
C1A C:HEM501 3.1 51.8 1.0
C4C C:HEM501 3.1 56.3 1.0
C4A C:HEM501 3.1 49.8 1.0
C4B C:HEM501 3.1 55.0 1.0
C1D C:HEM501 3.1 50.4 1.0
C1B C:HEM501 3.1 53.7 1.0
C04 C:8J4503 3.2 74.5 1.0
CB C:CYS184 3.3 46.8 1.0
CHA C:HEM501 3.4 53.3 1.0
CHC C:HEM501 3.4 59.5 1.0
CHD C:HEM501 3.5 53.1 1.0
CHB C:HEM501 3.5 51.7 1.0
C03 C:8J4503 3.6 74.0 1.0
C05 C:8J4503 4.0 76.8 1.0
CA C:CYS184 4.1 41.2 1.0
C2C C:HEM501 4.3 63.6 1.0
C3C C:HEM501 4.3 59.4 1.0
C3A C:HEM501 4.3 47.7 1.0
C2A C:HEM501 4.3 54.3 1.0
C3D C:HEM501 4.3 51.8 1.0
C3B C:HEM501 4.4 53.0 1.0
C2D C:HEM501 4.4 46.5 1.0
C2B C:HEM501 4.4 54.7 1.0
C06 C:8J4503 4.4 77.7 1.0
C02 C:8J4503 4.4 73.9 1.0
NE1 C:TRP178 4.6 49.0 1.0
C10 C:8J4503 4.8 76.7 1.0
N C:GLY186 4.8 47.9 1.0
C C:CYS184 4.8 40.2 1.0
N C:VAL185 4.9 30.9 1.0
N01 C:8J4503 5.0 76.5 1.0

Iron binding site 4 out of 4 in 5uo9

Go back to Iron Binding Sites List in 5uo9
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:34.3
occ:1.00
 FE D:HEM501 0.0 34.3 1.0
ND D:HEM501 2.0 40.5 1.0
NA D:HEM501 2.1 47.5 1.0
NC D:HEM501 2.1 45.5 1.0
NB D:HEM501 2.1 34.6 1.0
SG D:CYS184 2.2 30.4 1.0
C04 D:8J4503 3.0 48.0 1.0
C1D D:HEM501 3.0 39.1 1.0
C4C D:HEM501 3.0 41.2 1.0
C4A D:HEM501 3.0 40.6 1.0
C1B D:HEM501 3.1 39.5 1.0
C4D D:HEM501 3.1 46.8 1.0
C1A D:HEM501 3.1 48.2 1.0
C1C D:HEM501 3.2 44.3 1.0
C4B D:HEM501 3.2 37.5 1.0
CHD D:HEM501 3.3 40.4 1.0
CHB D:HEM501 3.4 38.2 1.0
CB D:CYS184 3.4 32.2 1.0
C03 D:8J4503 3.5 51.6 1.0
CHA D:HEM501 3.5 50.9 1.0
CHC D:HEM501 3.6 43.4 1.0
C05 D:8J4503 3.8 53.5 1.0
C06 D:8J4503 4.1 59.4 1.0
CA D:CYS184 4.1 30.6 1.0
C2D D:HEM501 4.2 38.9 1.0
C3A D:HEM501 4.3 43.5 1.0
C3D D:HEM501 4.3 42.6 1.0
C2A D:HEM501 4.3 46.7 1.0
C3C D:HEM501 4.3 42.4 1.0
C2B D:HEM501 4.3 41.8 1.0
C2C D:HEM501 4.4 41.9 1.0
C3B D:HEM501 4.4 38.9 1.0
NE1 D:TRP178 4.5 30.7 1.0
C02 D:8J4503 4.5 50.9 1.0
N D:GLY186 4.8 32.8 1.0
C10 D:8J4503 4.8 57.5 1.0
C D:CYS184 4.8 33.2 1.0
N D:VAL185 4.9 35.2 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 09:58:36 2024

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