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Iron in PDB 5uoc: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile, PDB code: 5uoc 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) 39.06 / 2.20
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 58.961, 153.504, 109.734, 90.00, 90.62, 90.00
R / Rfree (%) 21.2 / 28.8

Other elements in 5uoc:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile also contains other interesting chemical elements:

Zinc (Zn) 4 atoms
Gadolinium (Gd) 4 atoms
Chlorine (Cl) 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 (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile (pdb code 5uoc). 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 (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile, PDB code: 5uoc:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5uoc

Go back to Iron Binding Sites List in 5uoc
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)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 (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:66.1
occ:1.00
 FE A:HEM501 0.0 66.1 1.0
NC A:HEM501 2.1 91.5 1.0
NB A:HEM501 2.1 74.7 1.0
NA A:HEM501 2.1 65.3 1.0
ND A:HEM501 2.1 77.6 1.0
SG A:CYS184 2.3 65.0 1.0
C1B A:HEM501 3.1 66.6 1.0
C1C A:HEM501 3.1 79.5 1.0
C4B A:HEM501 3.1 66.3 1.0
C4C A:HEM501 3.1 82.1 1.0
C4A A:HEM501 3.1 68.1 1.0
C1D A:HEM501 3.1 82.2 1.0
C1A A:HEM501 3.1 70.4 1.0
C4D A:HEM501 3.1 80.9 1.0
CB A:CYS184 3.3 62.8 1.0
CHB A:HEM501 3.4 68.9 1.0
CHD A:HEM501 3.4 81.1 1.0
CHC A:HEM501 3.4 63.7 1.0
CHA A:HEM501 3.5 80.2 1.0
C04 A:8FD503 3.8 63.8 1.0
C05 A:8FD503 3.9 78.3 1.0
CA A:CYS184 4.0 62.9 1.0
C03 A:8FD503 4.1 63.6 1.0
C11 A:8FD503 4.1 67.3 1.0
C2B A:HEM501 4.3 69.4 1.0
C3B A:HEM501 4.3 71.8 1.0
C2C A:HEM501 4.3 74.2 1.0
C3C A:HEM501 4.3 75.7 1.0
C3A A:HEM501 4.3 66.3 1.0
C2A A:HEM501 4.4 73.6 1.0
C06 A:8FD503 4.4 83.4 1.0
C10 A:8FD503 4.4 80.5 1.0
C2D A:HEM501 4.4 79.1 1.0
C3D A:HEM501 4.4 83.4 1.0
C02 A:8FD503 4.5 68.1 1.0
N01 A:8FD503 4.6 73.5 1.0
NE1 A:TRP178 4.6 56.5 1.0
C A:CYS184 4.7 63.4 1.0
N A:VAL185 4.8 64.2 1.0
N A:GLY186 4.8 52.1 1.0

Iron binding site 2 out of 4 in 5uoc

Go back to Iron Binding Sites List in 5uoc
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)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 (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:45.5
occ:1.00
 FE B:HEM501 0.0 45.5 1.0
ND B:HEM501 2.0 48.6 1.0
NC B:HEM501 2.1 60.1 1.0
NB B:HEM501 2.1 51.6 1.0
NA B:HEM501 2.2 43.0 1.0
SG B:CYS184 2.3 42.7 1.0
C1D B:HEM501 3.0 58.3 1.0
C4C B:HEM501 3.1 48.5 1.0
C4D B:HEM501 3.1 56.9 1.0
C4B B:HEM501 3.1 56.0 1.0
C1B B:HEM501 3.1 50.2 1.0
C1C B:HEM501 3.1 57.8 1.0
C1A B:HEM501 3.1 49.6 1.0
C4A B:HEM501 3.2 49.0 1.0
CHD B:HEM501 3.4 43.1 1.0
CB B:CYS184 3.5 42.9 1.0
CHC B:HEM501 3.5 60.1 1.0
CHA B:HEM501 3.5 48.8 1.0
CHB B:HEM501 3.5 39.4 1.0
C04 B:8FD503 3.7 65.9 1.0
C05 B:8FD503 3.8 64.7 1.0
C11 B:8FD503 4.1 47.7 1.0
C06 B:8FD503 4.1 68.9 1.0
C03 B:8FD503 4.1 61.4 1.0
CA B:CYS184 4.2 54.3 1.0
C10 B:8FD503 4.2 62.9 1.0
C2D B:HEM501 4.3 57.4 1.0
C3D B:HEM501 4.3 50.1 1.0
C3C B:HEM501 4.3 63.1 1.0
C2C B:HEM501 4.3 59.5 1.0
C2B B:HEM501 4.3 59.9 1.0
C3B B:HEM501 4.3 59.5 1.0
C2A B:HEM501 4.4 55.9 1.0
C3A B:HEM501 4.4 58.6 1.0
NE1 B:TRP178 4.4 55.4 1.0
C02 B:8FD503 4.5 60.4 1.0
N01 B:8FD503 4.6 56.6 1.0
C07 B:8FD503 4.8 63.0 1.0
C09 B:8FD503 4.9 64.6 1.0

Iron binding site 3 out of 4 in 5uoc

Go back to Iron Binding Sites List in 5uoc
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)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 (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:56.0
occ:1.00
 FE C:HEM501 0.0 56.0 1.0
NC C:HEM501 2.0 85.2 1.0
ND C:HEM501 2.1 81.5 1.0
NB C:HEM501 2.1 76.1 1.0
NA C:HEM501 2.2 79.1 1.0
SG C:CYS184 2.4 66.2 1.0
C4C C:HEM501 3.0 84.3 1.0
C1C C:HEM501 3.0 90.8 1.0
C1D C:HEM501 3.1 85.5 1.0
C1B C:HEM501 3.1 77.1 1.0
C4B C:HEM501 3.1 66.9 1.0
C4D C:HEM501 3.1 81.5 1.0
C4A C:HEM501 3.2 74.1 1.0
C1A C:HEM501 3.2 77.0 1.0
CB C:CYS184 3.2 51.8 1.0
CHD C:HEM501 3.3 89.9 1.0
CHC C:HEM501 3.4 76.5 1.0
CHB C:HEM501 3.5 70.5 1.0
CHA C:HEM501 3.5 74.2 1.0
CA C:CYS184 4.0 56.8 1.0
C04 C:8FD503 4.2 61.9 1.0
C3C C:HEM501 4.2 94.8 1.0
C2C C:HEM501 4.2 92.8 1.0
C03 C:8FD503 4.3 57.8 1.0
NE1 C:TRP178 4.3 48.4 1.0
C2B C:HEM501 4.3 68.7 1.0
C2D C:HEM501 4.3 72.2 1.0
C05 C:8FD503 4.3 77.4 1.0
C3B C:HEM501 4.3 73.3 1.0
C3D C:HEM501 4.3 76.8 1.0
C3A C:HEM501 4.4 62.6 1.0
C2A C:HEM501 4.4 71.5 1.0
C02 C:8FD503 4.5 64.1 1.0
C11 C:8FD503 4.6 62.0 1.0
C10 C:8FD503 4.6 75.1 1.0
N01 C:8FD503 4.7 71.0 1.0
N C:GLY186 4.8 45.4 1.0
C C:CYS184 4.8 59.3 1.0
C06 C:8FD503 4.9 87.0 1.0
CD1 C:TRP178 5.0 64.2 1.0

Iron binding site 4 out of 4 in 5uoc

Go back to Iron Binding Sites List in 5uoc
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)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 (S)-3-[(2-Amino-4-Methylquinolin-7-Yl)Methoxy]-5-(2- (Methylamino)Propyl)Benzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:43.7
occ:1.00
 FE D:HEM501 0.0 43.7 1.0
ND D:HEM501 2.1 59.4 1.0
NA D:HEM501 2.1 57.4 1.0
NC D:HEM501 2.1 63.7 1.0
NB D:HEM501 2.1 57.1 1.0
SG D:CYS184 2.4 40.0 1.0
C4A D:HEM501 3.0 51.5 1.0
C1D D:HEM501 3.0 53.6 1.0
C4C D:HEM501 3.0 49.3 1.0
C1B D:HEM501 3.1 46.9 1.0
C4D D:HEM501 3.1 61.9 1.0
C1A D:HEM501 3.1 51.9 1.0
C1C D:HEM501 3.2 62.5 1.0
C4B D:HEM501 3.2 61.1 1.0
CHD D:HEM501 3.3 47.2 1.0
CHB D:HEM501 3.4 43.3 1.0
CB D:CYS184 3.4 39.8 1.0
CHA D:HEM501 3.5 58.9 1.0
CHC D:HEM501 3.5 60.7 1.0
C05 D:8FD503 3.8 49.0 1.0
C04 D:8FD503 3.8 51.0 1.0
C06 D:8FD503 4.1 52.3 1.0
C11 D:8FD503 4.2 60.0 1.0
C10 D:8FD503 4.2 57.7 1.0
C03 D:8FD503 4.2 43.2 1.0
CA D:CYS184 4.2 43.9 1.0
C3A D:HEM501 4.2 58.6 1.0
C2D D:HEM501 4.3 58.0 1.0
C3C D:HEM501 4.3 67.4 1.0
C2A D:HEM501 4.3 57.2 1.0
C2B D:HEM501 4.3 57.0 1.0
C3D D:HEM501 4.3 52.0 1.0
C2C D:HEM501 4.3 43.5 1.0
C3B D:HEM501 4.4 61.1 1.0
N01 D:8FD503 4.5 49.2 1.0
C02 D:8FD503 4.5 50.1 1.0
NE1 D:TRP178 4.7 59.4 1.0
C07 D:8FD503 4.7 61.2 1.0
C09 D:8FD503 4.8 56.7 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 09:59:43 2024

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