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Iron in PDB 5vvb: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile, PDB code: 5vvb 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) 55.30 / 2.15
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.310, 153.050, 108.681, 90.00, 90.75, 90.00
R / Rfree (%) 20.2 / 26.8

Other elements in 5vvb:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile also contains other interesting chemical elements:

Zinc (Zn) 2 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 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile (pdb code 5vvb). 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-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile, PDB code: 5vvb:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5vvb

Go back to Iron Binding Sites List in 5vvb
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile


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-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:30.9
occ:1.00
 FE A:HEM501 0.0 30.9 1.0
NB A:HEM501 2.0 39.8 1.0
NC A:HEM501 2.1 44.1 1.0
NA A:HEM501 2.1 38.7 1.0
ND A:HEM501 2.2 40.6 1.0
SG A:CYS184 2.4 32.4 1.0
C4B A:HEM501 3.0 44.0 1.0
C1C A:HEM501 3.0 42.4 1.0
C1B A:HEM501 3.1 43.1 1.0
C4C A:HEM501 3.1 39.2 1.0
C1A A:HEM501 3.2 41.1 1.0
C4A A:HEM501 3.2 32.5 1.0
C4D A:HEM501 3.2 44.1 1.0
C1D A:HEM501 3.2 39.7 1.0
C04 A:9P7503 3.2 40.2 1.0
C03 A:9P7503 3.3 32.5 1.0
CHC A:HEM501 3.3 34.7 1.0
CB A:CYS184 3.3 36.7 1.0
CHB A:HEM501 3.5 31.0 1.0
CHA A:HEM501 3.5 35.6 1.0
CHD A:HEM501 3.5 42.2 1.0
CA A:CYS184 4.1 27.8 1.0
C05 A:9P7503 4.1 41.9 1.0
C3B A:HEM501 4.2 36.9 1.0
C2B A:HEM501 4.2 36.9 1.0
C02 A:9P7503 4.3 34.5 1.0
C2C A:HEM501 4.3 48.3 1.0
NE1 A:TRP178 4.3 47.5 1.0
C3C A:HEM501 4.3 45.1 1.0
C2A A:HEM501 4.4 36.5 1.0
C3A A:HEM501 4.4 31.3 1.0
C3D A:HEM501 4.4 43.5 1.0
C2D A:HEM501 4.4 37.7 1.0
N A:GLY186 4.6 29.8 1.0
C06 A:9P7503 4.8 39.8 1.0
C A:CYS184 4.8 27.4 1.0
N A:VAL185 4.9 23.9 1.0
CD1 A:TRP178 4.9 42.6 1.0
C10 A:9P7503 4.9 38.1 1.0
CA A:GLY186 4.9 30.6 1.0
N02 A:9P7503 4.9 27.2 1.0
N01 A:9P7503 5.0 27.8 1.0

Iron binding site 2 out of 4 in 5vvb

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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 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile


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-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:38.1
occ:1.00
 FE B:HEM501 0.0 38.1 1.0
NA B:HEM501 2.0 40.0 1.0
NB B:HEM501 2.1 24.7 1.0
ND B:HEM501 2.1 32.3 1.0
SG B:CYS184 2.2 22.6 1.0
NC B:HEM501 2.2 16.9 1.0
C4A B:HEM501 3.0 25.6 1.0
C1A B:HEM501 3.0 24.1 1.0
C1B B:HEM501 3.0 21.8 1.0
C1D B:HEM501 3.1 25.6 1.0
C04 B:9P7503 3.1 22.6 1.0
C4C B:HEM501 3.1 20.5 1.0
C4D B:HEM501 3.1 21.9 1.0
C4B B:HEM501 3.2 19.1 1.0
C1C B:HEM501 3.2 19.2 1.0
CHB B:HEM501 3.3 18.9 1.0
CHD B:HEM501 3.4 17.2 1.0
CB B:CYS184 3.4 18.9 1.0
C03 B:9P7503 3.4 29.1 1.0
CHA B:HEM501 3.5 20.6 1.0
CHC B:HEM501 3.6 20.6 1.0
C05 B:9P7503 4.0 27.1 1.0
CA B:CYS184 4.1 15.7 1.0
C3A B:HEM501 4.2 34.5 1.0
C2A B:HEM501 4.2 29.6 1.0
C2B B:HEM501 4.3 30.7 1.0
C2D B:HEM501 4.4 28.1 1.0
C3D B:HEM501 4.4 31.6 1.0
C3B B:HEM501 4.4 27.0 1.0
C3C B:HEM501 4.4 17.3 1.0
C06 B:9P7503 4.4 25.5 1.0
C2C B:HEM501 4.4 17.4 1.0
C02 B:9P7503 4.5 31.6 1.0
NE1 B:TRP178 4.5 29.4 1.0
N B:GLY186 4.8 34.9 1.0
C10 B:9P7503 4.9 34.8 1.0
C B:CYS184 4.9 18.0 1.0
N B:VAL185 5.0 21.1 1.0

Iron binding site 3 out of 4 in 5vvb

Go back to Iron Binding Sites List in 5vvb
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile


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-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:87.1
occ:1.00
 FE C:HEM501 0.0 87.1 1.0
NA C:HEM501 2.1 58.5 1.0
ND C:HEM501 2.1 45.1 1.0
NC C:HEM501 2.1 58.6 1.0
NB C:HEM501 2.1 53.7 1.0
SG C:CYS184 2.3 36.1 1.0
C04 C:9P7503 3.0 35.5 1.0
C1A C:HEM501 3.1 44.7 1.0
C4D C:HEM501 3.1 41.5 1.0
C4A C:HEM501 3.1 52.0 1.0
C1D C:HEM501 3.1 49.5 1.0
C1B C:HEM501 3.1 50.2 1.0
C4C C:HEM501 3.1 50.9 1.0
C1C C:HEM501 3.1 45.8 1.0
C4B C:HEM501 3.1 50.5 1.0
C03 C:9P7503 3.2 30.1 1.0
CHA C:HEM501 3.4 39.7 1.0
CB C:CYS184 3.4 33.3 1.0
CHB C:HEM501 3.4 41.9 1.0
CHD C:HEM501 3.5 42.1 1.0
CHC C:HEM501 3.5 38.6 1.0
C05 C:9P7503 4.0 35.5 1.0
CA C:CYS184 4.2 37.0 1.0
NE1 C:TRP178 4.2 47.7 1.0
C02 C:9P7503 4.3 37.6 1.0
C3A C:HEM501 4.3 46.7 1.0
C2A C:HEM501 4.3 44.1 1.0
C3D C:HEM501 4.3 42.5 1.0
C2B C:HEM501 4.3 48.6 1.0
C2D C:HEM501 4.3 47.7 1.0
C3C C:HEM501 4.3 52.3 1.0
C2C C:HEM501 4.3 47.2 1.0
C3B C:HEM501 4.3 49.4 1.0
C06 C:9P7503 4.5 36.9 1.0
C10 C:9P7503 4.8 38.2 1.0
CD1 C:TRP178 4.9 44.9 1.0
C C:CYS184 4.9 35.4 1.0
N01 C:9P7503 4.9 39.2 1.0
N C:GLY186 4.9 35.4 1.0
N02 C:9P7503 5.0 34.5 1.0

Iron binding site 4 out of 4 in 5vvb

Go back to Iron Binding Sites List in 5vvb
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile


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-(2-(((2-Aminoquinolin-7-Yl)Methyl)Amino)Ethyl)-2- Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:23.9
occ:1.00
 FE D:HEM501 0.0 23.9 1.0
NA D:HEM501 2.1 25.2 1.0
ND D:HEM501 2.1 26.1 1.0
NB D:HEM501 2.1 14.7 1.0
NC D:HEM501 2.2 18.2 1.0
SG D:CYS184 2.3 23.2 1.0
C4A D:HEM501 3.1 23.1 1.0
C1A D:HEM501 3.1 17.2 1.0
C1B D:HEM501 3.1 19.2 1.0
C4D D:HEM501 3.1 31.9 1.0
C1D D:HEM501 3.1 24.7 1.0
C4B D:HEM501 3.1 27.7 1.0
C4C D:HEM501 3.1 29.4 1.0
C1C D:HEM501 3.2 23.9 1.0
C04 D:9P7503 3.2 23.6 1.0
CHB D:HEM501 3.4 13.2 1.0
CHA D:HEM501 3.4 20.4 1.0
CB D:CYS184 3.4 23.6 1.0
CHD D:HEM501 3.5 23.7 1.0
CHC D:HEM501 3.5 15.2 1.0
C03 D:9P7503 3.5 23.3 1.0
C05 D:9P7503 4.1 25.2 1.0
CA D:CYS184 4.1 26.4 1.0
C2B D:HEM501 4.3 21.7 1.0
C3A D:HEM501 4.3 21.9 1.0
NE1 D:TRP178 4.3 27.9 1.0
C2A D:HEM501 4.3 24.0 1.0
C3D D:HEM501 4.3 21.2 1.0
C2D D:HEM501 4.3 26.3 1.0
C3B D:HEM501 4.3 21.6 1.0
C3C D:HEM501 4.4 28.2 1.0
C2C D:HEM501 4.4 22.7 1.0
C06 D:9P7503 4.5 28.6 1.0
C02 D:9P7503 4.5 17.4 1.0
N D:GLY186 4.7 30.5 1.0
N D:VAL185 4.8 32.7 1.0
C D:CYS184 4.8 21.4 1.0
C10 D:9P7503 4.9 29.1 1.0
CD1 D:TRP178 5.0 20.9 1.0

Reference:

A.V.Pensa, M.A.Cinelli, H.Li, G.Chreifi, P.Mukherjee, L.J.Roman, P.Martasek, T.L.Poulos, R.B.Silverman. Hydrophilic, Potent, and Selective 7-Substituted 2-Aminoquinolines As Improved Human Neuronal Nitric Oxide Synthase Inhibitors. J. Med. Chem. V. 60 7146 2017.
ISSN: ISSN 1520-4804
PubMed: 28776992
DOI: 10.1021/ACS.JMEDCHEM.7B00835
Page generated: Tue Aug 6 11:01:49 2024

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