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Iron in PDB 5vv6: Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine

Enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine

All present enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine, PDB code: 5vv6 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) 39.17 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.800, 106.196, 156.672, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 22

Other elements in 5vv6:

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine (pdb code 5vv6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine, PDB code: 5vv6:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5vv6

Go back to Iron Binding Sites List in 5vv6
Iron binding site 1 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)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 Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:22.1
occ:1.00
FE A:HEM501 0.0 22.1 1.0
NC A:HEM501 2.1 21.7 1.0
ND A:HEM501 2.1 17.8 1.0
NA A:HEM501 2.1 23.3 1.0
NB A:HEM501 2.1 18.1 1.0
SG A:CYS186 2.3 24.9 1.0
C4C A:HEM501 3.1 21.4 1.0
C1D A:HEM501 3.1 27.3 1.0
C1A A:HEM501 3.1 25.0 1.0
C4D A:HEM501 3.1 20.0 1.0
C1C A:HEM501 3.1 21.0 1.0
C4B A:HEM501 3.1 25.8 1.0
C1B A:HEM501 3.1 15.5 1.0
C4A A:HEM501 3.1 21.5 1.0
C04 A:P64503 3.2 16.1 1.0
CB A:CYS186 3.4 22.8 1.0
CHD A:HEM501 3.4 24.7 1.0
C03 A:P64503 3.4 21.0 1.0
CHA A:HEM501 3.5 18.7 1.0
CHC A:HEM501 3.5 19.9 1.0
CHB A:HEM501 3.5 18.9 1.0
C05 A:P64503 4.1 21.3 1.0
CA A:CYS186 4.1 17.9 1.0
NE1 A:TRP180 4.2 28.9 1.0
C3C A:HEM501 4.3 24.6 1.0
C2C A:HEM501 4.3 24.4 1.0
C2D A:HEM501 4.3 24.9 1.0
C3D A:HEM501 4.3 18.9 1.0
C2B A:HEM501 4.3 15.9 1.0
C2A A:HEM501 4.3 23.7 1.0
C3B A:HEM501 4.3 20.9 1.0
C3A A:HEM501 4.4 19.4 1.0
C02 A:P64503 4.4 27.7 1.0
C06 A:P64503 4.6 23.2 1.0
N A:GLY188 4.7 25.0 1.0
C A:CYS186 4.8 24.5 1.0
CD1 A:TRP180 4.9 22.0 1.0
N A:VAL187 4.9 21.7 1.0
C10 A:P64503 4.9 26.4 1.0

Iron binding site 2 out of 2 in 5vv6

Go back to Iron Binding Sites List in 5vv6
Iron binding site 2 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)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 Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((4-(Dimethylamino)Phenethyl)Amino)Methyl)Quinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:24.2
occ:1.00
FE B:HEM501 0.0 24.2 1.0
ND B:HEM501 2.1 19.3 1.0
NC B:HEM501 2.1 23.0 1.0
NB B:HEM501 2.1 21.1 1.0
NA B:HEM501 2.1 24.3 1.0
SG B:CYS186 2.3 23.9 1.0
C1D B:HEM501 3.1 25.5 1.0
C4C B:HEM501 3.1 21.9 1.0
C4D B:HEM501 3.1 22.6 1.0
C04 B:P64503 3.1 19.9 1.0
C1B B:HEM501 3.1 25.0 1.0
C1A B:HEM501 3.1 24.0 1.0
C4A B:HEM501 3.1 21.6 1.0
C4B B:HEM501 3.1 26.8 1.0
C1C B:HEM501 3.2 25.2 1.0
C03 B:P64503 3.4 25.0 1.0
CB B:CYS186 3.4 24.8 1.0
CHD B:HEM501 3.4 21.7 1.0
CHA B:HEM501 3.5 16.4 1.0
CHB B:HEM501 3.5 27.1 1.0
CHC B:HEM501 3.5 23.6 1.0
C05 B:P64503 4.0 30.2 1.0
CA B:CYS186 4.1 23.3 1.0
NE1 B:TRP180 4.2 24.9 1.0
C2D B:HEM501 4.3 23.7 1.0
C3D B:HEM501 4.3 21.7 1.0
C3C B:HEM501 4.3 24.3 1.0
C2B B:HEM501 4.3 23.4 1.0
C2A B:HEM501 4.4 28.1 1.0
C3A B:HEM501 4.4 23.0 1.0
C3B B:HEM501 4.4 25.4 1.0
C2C B:HEM501 4.4 24.5 1.0
C02 B:P64503 4.4 27.4 1.0
C06 B:P64503 4.6 28.9 1.0
N B:GLY188 4.7 20.6 1.0
C B:CYS186 4.9 17.9 1.0
CD1 B:TRP180 4.9 26.1 1.0
C10 B:P64503 4.9 25.9 1.0
N B:VAL187 4.9 21.2 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: Sun Dec 13 16:15:36 2020

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