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Iron in PDB 5vv7: Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine

Enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine

All present enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((3-(Pyridin-3-Yl)Propyl)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-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine, PDB code: 5vv7 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) 63.11 / 2.20
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.530, 106.700, 156.550, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 23.5

Other elements in 5vv7:

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((3-(Pyridin-3-Yl)Propyl)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-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine (pdb code 5vv7). 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-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine, PDB code: 5vv7:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5vv7

Go back to Iron Binding Sites List in 5vv7
Iron binding site 1 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((3-(Pyridin-3-Yl)Propyl)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-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:35.5
occ:1.00
 FE A:HEM501 0.0 35.5 1.0
NB A:HEM501 2.0 25.4 1.0
ND A:HEM501 2.1 25.2 1.0
NA A:HEM501 2.1 37.5 1.0
NC A:HEM501 2.1 33.5 1.0
SG A:CYS186 2.4 37.9 1.0
C4D A:HEM501 3.0 29.1 1.0
C4B A:HEM501 3.0 33.2 1.0
C1A A:HEM501 3.1 33.5 1.0
C1C A:HEM501 3.1 30.3 1.0
C1B A:HEM501 3.1 31.9 1.0
C1D A:HEM501 3.1 28.2 1.0
C4A A:HEM501 3.1 34.9 1.0
C4C A:HEM501 3.1 32.5 1.0
C04 A:XH8503 3.2 33.5 1.0
CB A:CYS186 3.3 32.2 1.0
C03 A:XH8503 3.3 34.7 1.0
CHA A:HEM501 3.4 30.6 1.0
CHC A:HEM501 3.4 31.2 1.0
CHB A:HEM501 3.5 35.4 1.0
CHD A:HEM501 3.5 33.1 1.0
C05 A:XH8503 4.1 37.2 1.0
CA A:CYS186 4.1 33.5 1.0
C3D A:HEM501 4.3 33.3 1.0
C3B A:HEM501 4.3 36.0 1.0
C02 A:XH8503 4.3 37.9 1.0
C2B A:HEM501 4.3 33.4 1.0
C2A A:HEM501 4.3 35.9 1.0
C2C A:HEM501 4.3 28.5 1.0
NE1 A:TRP180 4.3 35.9 1.0
C3A A:HEM501 4.3 32.3 1.0
C2D A:HEM501 4.3 30.1 1.0
C3C A:HEM501 4.4 28.6 1.0
C06 A:XH8503 4.7 41.5 1.0
N A:GLY188 4.7 35.2 1.0
C A:CYS186 4.8 39.5 1.0
N A:VAL187 4.9 33.4 1.0
C21 A:XH8503 4.9 35.1 1.0
CD1 A:TRP180 4.9 38.5 1.0
N22 A:XH8503 5.0 37.4 1.0

Iron binding site 2 out of 2 in 5vv7

Go back to Iron Binding Sites List in 5vv7
Iron binding site 2 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(((3-(Pyridin-3-Yl)Propyl)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-(((3-(Pyridin-3-Yl)Propyl)Amino)Methyl)Quinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:39.6
occ:1.00
 FE B:HEM501 0.0 39.6 1.0
ND B:HEM501 2.1 45.9 1.0
NB B:HEM501 2.1 38.2 1.0
NC B:HEM501 2.1 35.9 1.0
NA B:HEM501 2.1 43.3 1.0
SG B:CYS186 2.3 36.6 1.0
C4D B:HEM501 3.0 45.9 1.0
C4B B:HEM501 3.1 39.0 1.0
C1D B:HEM501 3.1 44.3 1.0
C1A B:HEM501 3.1 40.0 1.0
C1C B:HEM501 3.1 37.8 1.0
C1B B:HEM501 3.1 39.6 1.0
C4C B:HEM501 3.1 39.8 1.0
C04 B:XH8503 3.1 35.6 1.0
C4A B:HEM501 3.2 37.8 1.0
CB B:CYS186 3.4 45.6 1.0
C03 B:XH8503 3.4 39.7 1.0
CHA B:HEM501 3.4 40.8 1.0
CHC B:HEM501 3.4 36.9 1.0
CHD B:HEM501 3.5 43.7 1.0
CHB B:HEM501 3.5 39.8 1.0
C05 B:XH8503 4.1 44.1 1.0
CA B:CYS186 4.2 40.9 1.0
NE1 B:TRP180 4.2 33.8 1.0
C3D B:HEM501 4.3 41.5 1.0
C3B B:HEM501 4.3 37.4 1.0
C2B B:HEM501 4.3 38.2 1.0
C2D B:HEM501 4.3 39.4 1.0
C2A B:HEM501 4.3 38.9 1.0
C2C B:HEM501 4.3 38.2 1.0
C3C B:HEM501 4.4 42.9 1.0
C3A B:HEM501 4.4 38.7 1.0
C02 B:XH8503 4.4 45.4 1.0
C06 B:XH8503 4.6 45.5 1.0
N B:GLY188 4.8 36.7 1.0
CD1 B:TRP180 4.9 39.6 1.0
C B:CYS186 4.9 35.9 1.0
N B:VAL187 4.9 35.2 1.0
C21 B:XH8503 4.9 45.6 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 11:01:42 2024

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