Atomistry » Iron » PDB 6pn8-6prr » 6poy
Atomistry »
  Iron »
    PDB 6pn8-6prr »
      6poy »

Iron in PDB 6poy: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine, PDB code: 6poy 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) 52.60 / 2.30
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.689, 153.410, 109.188, 90.00, 90.60, 90.00
R / Rfree (%) 19.8 / 26.1

Other elements in 6poy:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine 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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine (pdb code 6poy). 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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine, PDB code: 6poy:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:50.0
occ:1.00
 FE A:HEM501 0.0 50.0 1.0
NB A:HEM501 2.1 56.0 1.0
NC A:HEM501 2.1 62.1 1.0
NA A:HEM501 2.1 52.3 1.0
ND A:HEM501 2.1 50.0 1.0
SG A:CYS184 2.3 37.3 1.0
C1B A:HEM501 3.0 63.1 1.0
C4A A:HEM501 3.0 54.7 1.0
C4C A:HEM501 3.1 62.5 1.0
C1D A:HEM501 3.1 57.3 1.0
C4B A:HEM501 3.1 53.7 1.0
C1C A:HEM501 3.1 57.9 1.0
C1A A:HEM501 3.1 47.0 1.0
C4D A:HEM501 3.2 56.8 1.0
CB A:CYS184 3.3 42.2 1.0
CHB A:HEM501 3.4 62.0 1.0
CHD A:HEM501 3.4 51.2 1.0
CHC A:HEM501 3.5 55.7 1.0
CHA A:HEM501 3.5 54.0 1.0
C04 A:OSG503 3.8 55.6 1.0
C05 A:OSG503 3.9 58.7 1.0
CA A:CYS184 4.0 42.9 1.0
C11 A:OSG503 4.0 58.0 1.0
C03 A:OSG503 4.1 48.8 1.0
C2B A:HEM501 4.3 55.2 1.0
C06 A:OSG503 4.3 57.8 1.0
C3A A:HEM501 4.3 56.6 1.0
C3B A:HEM501 4.3 50.2 1.0
C3C A:HEM501 4.3 63.5 1.0
C2A A:HEM501 4.3 60.0 1.0
C2C A:HEM501 4.3 62.4 1.0
C2D A:HEM501 4.3 57.2 1.0
C3D A:HEM501 4.4 62.5 1.0
C10 A:OSG503 4.4 54.3 1.0
NE1 A:TRP178 4.4 55.5 1.0
C02 A:OSG503 4.6 47.2 1.0
N01 A:OSG503 4.7 50.7 1.0
C A:CYS184 4.9 50.6 1.0
N A:GLY186 4.9 40.8 1.0
N A:VAL185 5.0 50.7 1.0
C07 A:OSG503 5.0 58.1 1.0

Iron binding site 2 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:29.2
occ:1.00
 FE B:HEM501 0.0 29.2 1.0
NA B:HEM501 2.0 42.9 1.0
NB B:HEM501 2.1 40.6 1.0
ND B:HEM501 2.2 42.1 1.0
NC B:HEM501 2.2 39.8 1.0
SG B:CYS184 2.2 22.3 1.0
C4A B:HEM501 3.0 35.4 1.0
C1B B:HEM501 3.0 36.0 1.0
C1A B:HEM501 3.1 34.4 1.0
C4B B:HEM501 3.1 37.5 1.0
C1D B:HEM501 3.1 37.3 1.0
C4D B:HEM501 3.2 43.1 1.0
C4C B:HEM501 3.2 32.2 1.0
C1C B:HEM501 3.2 40.2 1.0
CHB B:HEM501 3.3 24.8 1.0
CB B:CYS184 3.3 22.1 1.0
CHD B:HEM501 3.5 32.0 1.0
CHC B:HEM501 3.5 36.0 1.0
CHA B:HEM501 3.5 35.9 1.0
C04 B:OSG503 4.0 35.7 1.0
C05 B:OSG503 4.0 28.0 1.0
CA B:CYS184 4.1 34.7 1.0
C3A B:HEM501 4.2 34.3 1.0
C2B B:HEM501 4.3 42.1 1.0
C2A B:HEM501 4.3 38.8 1.0
C11 B:OSG503 4.3 35.2 1.0
C03 B:OSG503 4.3 19.9 1.0
C3B B:HEM501 4.3 37.5 1.0
C06 B:OSG503 4.3 28.8 1.0
C2D B:HEM501 4.4 34.0 1.0
C3D B:HEM501 4.4 32.2 1.0
NE1 B:TRP178 4.4 27.1 1.0
C2C B:HEM501 4.4 42.2 1.0
C3C B:HEM501 4.4 41.6 1.0
C10 B:OSG503 4.4 34.6 1.0
C02 B:OSG503 4.7 25.2 1.0
N01 B:OSG503 4.8 31.8 1.0
N B:GLY186 4.8 24.7 1.0
C B:CYS184 4.8 31.1 1.0
N B:VAL185 4.9 27.1 1.0
C07 B:OSG503 5.0 27.6 1.0

Iron binding site 3 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine


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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:37.5
occ:1.00
 FE C:HEM501 0.0 37.5 1.0
ND C:HEM501 2.0 43.3 1.0
NA C:HEM501 2.1 46.2 1.0
NB C:HEM501 2.1 41.8 1.0
NC C:HEM501 2.1 48.7 1.0
SG C:CYS184 2.4 34.4 1.0
C4D C:HEM501 3.0 43.7 1.0
C1A C:HEM501 3.1 36.5 1.0
C4B C:HEM501 3.1 49.2 1.0
C4A C:HEM501 3.1 37.6 1.0
C1C C:HEM501 3.1 52.2 1.0
C1B C:HEM501 3.1 40.7 1.0
C1D C:HEM501 3.1 44.7 1.0
C4C C:HEM501 3.2 45.5 1.0
CHA C:HEM501 3.4 36.1 1.0
CB C:CYS184 3.4 31.5 1.0
CHC C:HEM501 3.4 49.4 1.0
CHB C:HEM501 3.5 27.5 1.0
CHD C:HEM501 3.5 38.2 1.0
C04 C:OSG503 3.8 47.7 1.0
C05 C:OSG503 4.0 41.7 1.0
C03 C:OSG503 4.0 48.5 1.0
C11 C:OSG503 4.1 42.7 1.0
CA C:CYS184 4.1 30.4 1.0
C3D C:HEM501 4.3 41.0 1.0
C2A C:HEM501 4.3 41.3 1.0
C2D C:HEM501 4.3 33.1 1.0
C3A C:HEM501 4.3 37.4 1.0
C2B C:HEM501 4.3 38.8 1.0
C3B C:HEM501 4.3 42.0 1.0
C2C C:HEM501 4.3 51.6 1.0
NE1 C:TRP178 4.4 46.0 1.0
C3C C:HEM501 4.4 41.4 1.0
C06 C:OSG503 4.4 40.3 1.0
C10 C:OSG503 4.4 36.4 1.0
C02 C:OSG503 4.5 40.6 1.0
N01 C:OSG503 4.7 37.6 1.0
N C:GLY186 4.9 34.1 1.0
C C:CYS184 4.9 30.4 1.0
CD1 C:TRP178 4.9 38.4 1.0

Iron binding site 4 out of 4 in 6poy

Go back to Iron Binding Sites List in 6poy
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine


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 7-(3-(Aminomethyl)-4-Propoxyphenyl)-4-Methylquinolin-2- Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:20.5
occ:1.00
 FE D:HEM501 0.0 20.5 1.0
NA D:HEM501 2.0 38.9 1.0
ND D:HEM501 2.1 37.8 1.0
NB D:HEM501 2.2 31.7 1.0
NC D:HEM501 2.2 30.3 1.0
SG D:CYS184 2.2 19.9 1.0
C4A D:HEM501 3.0 32.7 1.0
C1A D:HEM501 3.0 43.4 1.0
C1B D:HEM501 3.1 34.6 1.0
C1D D:HEM501 3.1 33.7 1.0
C4D D:HEM501 3.1 44.4 1.0
C4C D:HEM501 3.2 32.1 1.0
C1C D:HEM501 3.2 40.5 1.0
C4B D:HEM501 3.2 30.7 1.0
CB D:CYS184 3.3 19.9 1.0
CHB D:HEM501 3.4 22.9 1.0
CHD D:HEM501 3.5 34.2 1.0
CHA D:HEM501 3.5 33.1 1.0
CHC D:HEM501 3.6 40.9 1.0
C04 D:OSG503 3.9 40.6 1.0
C05 D:OSG503 4.0 36.7 1.0
CA D:CYS184 4.0 28.1 1.0
C3A D:HEM501 4.2 39.0 1.0
C2A D:HEM501 4.2 35.4 1.0
C03 D:OSG503 4.2 31.6 1.0
C11 D:OSG503 4.3 37.4 1.0
C10 D:OSG503 4.3 34.2 1.0
C06 D:OSG503 4.3 36.2 1.0
C2D D:HEM501 4.3 32.5 1.0
C2B D:HEM501 4.4 38.8 1.0
C3D D:HEM501 4.4 33.7 1.0
C3C D:HEM501 4.4 42.6 1.0
C3B D:HEM501 4.4 36.1 1.0
C2C D:HEM501 4.4 36.6 1.0
C02 D:OSG503 4.6 34.1 1.0
NE1 D:TRP178 4.6 35.2 1.0
N01 D:OSG503 4.6 24.8 1.0
C D:CYS184 4.8 22.5 1.0
N D:GLY186 4.8 24.0 1.0
N D:VAL185 4.9 29.6 1.0
C07 D:OSG503 5.0 36.4 1.0

Reference:

M.A.Cinelli, C.T.Reidl, H.Li, G.Chreifi, T.L.Poulos, R.B.Silverman. First Contact: 7-Phenyl-2-Aminoquinolines, Potent and Selective Neuronal Nitric Oxide Synthase Inhibitors That Target An Isoform-Specific Aspartate. J.Med.Chem. 2020.
ISSN: ISSN 0022-2623
PubMed: 32302123
DOI: 10.1021/ACS.JMEDCHEM.9B01573
Page generated: Sun Dec 13 16:49:34 2020

Last articles

Zn in 7L0B
Zn in 7KZZ
Zn in 7KZL
Zn in 7L3O
Zn in 7L52
Zn in 7L6T
Zn in 7KZ7
Zn in 7L6R
Zn in 7KKM
Zn in 7KKQ
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy