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Iron in PDB 5vvc: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile, PDB code: 5vvc 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) 88.56 / 2.40
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.330, 152.620, 108.740, 90.00, 90.57, 90.00
R / Rfree (%) 20.6 / 27.2

Other elements in 5vvc:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile (pdb code 5vvc). 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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile, PDB code: 5vvc:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5vvc

Go back to Iron Binding Sites List in 5vvc
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:57.0
occ:1.00
 FE A:HEM501 0.0 57.0 1.0
NB A:HEM501 2.0 51.9 1.0
NC A:HEM501 2.0 59.5 1.0
NA A:HEM501 2.1 45.2 1.0
ND A:HEM501 2.1 52.2 1.0
SG A:CYS184 2.3 51.1 1.0
C1B A:HEM501 3.0 50.5 1.0
C4A A:HEM501 3.0 48.7 1.0
C4C A:HEM501 3.0 58.8 1.0
C1D A:HEM501 3.1 58.5 1.0
C1C A:HEM501 3.1 56.4 1.0
C4B A:HEM501 3.1 52.6 1.0
C4D A:HEM501 3.1 51.4 1.0
C1A A:HEM501 3.1 46.2 1.0
CB A:CYS184 3.3 50.0 1.0
CHB A:HEM501 3.3 49.2 1.0
CHD A:HEM501 3.4 60.1 1.0
CHC A:HEM501 3.5 53.2 1.0
CHA A:HEM501 3.5 48.3 1.0
C13 A:9OJ503 3.8 43.8 1.0
C14 A:9OJ503 3.8 47.3 1.0
C15 A:9OJ503 3.9 39.2 1.0
CA A:CYS184 4.2 47.3 1.0
C2B A:HEM501 4.2 47.4 1.0
C3C A:HEM501 4.3 55.1 1.0
C3A A:HEM501 4.3 47.6 1.0
C3B A:HEM501 4.3 51.0 1.0
C2C A:HEM501 4.3 58.1 1.0
C2D A:HEM501 4.3 59.5 1.0
C3D A:HEM501 4.3 54.6 1.0
C2A A:HEM501 4.3 47.5 1.0
NE1 A:TRP178 4.4 56.4 1.0
C12 A:9OJ503 4.5 46.3 1.0
C16 A:9OJ503 4.6 42.9 1.0
N A:GLY186 4.8 46.6 1.0
C A:CYS184 4.9 46.7 1.0
N A:VAL185 5.0 42.9 1.0

Iron binding site 2 out of 4 in 5vvc

Go back to Iron Binding Sites List in 5vvc
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:31.2
occ:1.00
 FE B:HEM501 0.0 31.2 1.0
NA B:HEM501 2.1 43.4 1.0
ND B:HEM501 2.1 45.5 1.0
NB B:HEM501 2.1 43.5 1.0
NC B:HEM501 2.1 49.6 1.0
SG B:CYS184 2.2 30.1 1.0
C4A B:HEM501 3.0 40.6 1.0
C1D B:HEM501 3.0 44.7 1.0
C4C B:HEM501 3.1 48.4 1.0
C1B B:HEM501 3.1 44.3 1.0
C1A B:HEM501 3.1 42.0 1.0
C4D B:HEM501 3.1 47.1 1.0
C4B B:HEM501 3.2 45.8 1.0
C1C B:HEM501 3.2 49.2 1.0
CB B:CYS184 3.3 45.5 1.0
CHD B:HEM501 3.3 45.4 1.0
CHB B:HEM501 3.3 40.3 1.0
CHA B:HEM501 3.5 43.8 1.0
CHC B:HEM501 3.6 48.9 1.0
C13 B:9OJ503 3.7 49.1 1.0
C14 B:9OJ503 3.7 53.7 1.0
C15 B:9OJ503 3.8 46.5 1.0
CA B:CYS184 4.0 42.1 1.0
C3A B:HEM501 4.3 39.9 1.0
C2D B:HEM501 4.3 44.5 1.0
C2A B:HEM501 4.3 39.9 1.0
NE1 B:TRP178 4.3 37.0 1.0
C2B B:HEM501 4.3 45.9 1.0
C3D B:HEM501 4.3 44.7 1.0
C3C B:HEM501 4.3 51.2 1.0
C3B B:HEM501 4.4 46.2 1.0
C2C B:HEM501 4.4 51.9 1.0
C12 B:9OJ503 4.4 45.0 1.0
C16 B:9OJ503 4.5 41.7 1.0
C B:CYS184 4.8 41.3 1.0
N B:GLY186 4.9 39.4 1.0
N B:VAL185 5.0 44.1 1.0
C11 B:9OJ503 5.0 39.7 1.0

Iron binding site 3 out of 4 in 5vvc

Go back to Iron Binding Sites List in 5vvc
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:44.1
occ:1.00
 FE C:HEM501 0.0 44.1 1.0
NC C:HEM501 2.0 54.0 1.0
NA C:HEM501 2.1 33.9 1.0
ND C:HEM501 2.1 47.3 1.0
NB C:HEM501 2.2 46.0 1.0
SG C:CYS184 2.4 43.3 1.0
C4C C:HEM501 3.0 53.1 1.0
C1C C:HEM501 3.0 56.6 1.0
C1D C:HEM501 3.1 50.5 1.0
C1A C:HEM501 3.1 40.2 1.0
C4D C:HEM501 3.1 47.2 1.0
C4A C:HEM501 3.1 35.5 1.0
C4B C:HEM501 3.2 48.1 1.0
C1B C:HEM501 3.2 45.4 1.0
CB C:CYS184 3.3 35.7 1.0
CHD C:HEM501 3.4 52.4 1.0
CHA C:HEM501 3.5 42.3 1.0
CHC C:HEM501 3.5 51.2 1.0
CHB C:HEM501 3.5 40.6 1.0
C15 C:9OJ503 3.8 56.1 1.0
C13 C:9OJ503 3.9 57.2 1.0
C14 C:9OJ503 3.9 56.2 1.0
CA C:CYS184 4.1 38.6 1.0
C3C C:HEM501 4.2 53.6 1.0
C2C C:HEM501 4.2 57.7 1.0
C2A C:HEM501 4.3 38.9 1.0
C2D C:HEM501 4.3 47.9 1.0
C3A C:HEM501 4.4 35.7 1.0
C3D C:HEM501 4.4 49.5 1.0
C3B C:HEM501 4.4 49.2 1.0
C2B C:HEM501 4.4 45.7 1.0
NE1 C:TRP178 4.4 49.3 1.0
C16 C:9OJ503 4.5 53.6 1.0
C12 C:9OJ503 4.5 58.4 1.0
N C:GLY186 4.6 45.3 1.0
C C:CYS184 4.8 37.5 1.0
N C:VAL185 4.9 37.3 1.0
CA C:GLY186 4.9 47.6 1.0
CD1 C:TRP178 5.0 49.1 1.0

Iron binding site 4 out of 4 in 5vvc

Go back to Iron Binding Sites List in 5vvc
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-(2-(((2-Amino-4-Methylquinolin-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-Amino-4-Methylquinolin-7-Yl)Methyl)Amino) Ethyl)-2-Methylbenzonitrile within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:33.3
occ:1.00
 FE D:HEM501 0.0 33.3 1.0
NA D:HEM501 2.0 40.9 1.0
ND D:HEM501 2.1 37.7 1.0
NC D:HEM501 2.1 37.8 1.0
NB D:HEM501 2.1 40.4 1.0
SG D:CYS184 2.2 28.7 1.0
C1D D:HEM501 3.0 36.7 1.0
C4A D:HEM501 3.0 36.4 1.0
C4C D:HEM501 3.0 34.3 1.0
C1A D:HEM501 3.1 42.3 1.0
C1B D:HEM501 3.1 40.2 1.0
C4D D:HEM501 3.1 40.2 1.0
C1C D:HEM501 3.2 39.0 1.0
C4B D:HEM501 3.2 41.0 1.0
CHD D:HEM501 3.3 34.1 1.0
CB D:CYS184 3.3 41.1 1.0
CHB D:HEM501 3.4 36.2 1.0
CHA D:HEM501 3.5 43.0 1.0
C14 D:9OJ503 3.5 49.0 1.0
CHC D:HEM501 3.6 41.0 1.0
C13 D:9OJ503 3.7 46.5 1.0
C15 D:9OJ503 3.8 41.1 1.0
CA D:CYS184 4.1 33.3 1.0
C3A D:HEM501 4.3 36.3 1.0
C2D D:HEM501 4.3 38.9 1.0
C2A D:HEM501 4.3 36.4 1.0
C3C D:HEM501 4.3 37.9 1.0
C3D D:HEM501 4.3 38.4 1.0
C2B D:HEM501 4.3 40.7 1.0
C2C D:HEM501 4.4 38.4 1.0
C3B D:HEM501 4.4 40.2 1.0
C12 D:9OJ503 4.5 45.8 1.0
NE1 D:TRP178 4.6 40.0 1.0
C16 D:9OJ503 4.6 36.1 1.0
N D:GLY186 4.7 39.8 1.0
C D:CYS184 4.8 34.8 1.0
N D:VAL185 5.0 36.8 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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