Atomistry » Iron » PDB 5ug2-5utc » 5uo9
Atomistry »
  Iron »
    PDB 5ug2-5utc »
      5uo9 »

Iron in PDB 5uo9: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine, PDB code: 5uo9 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) 38.87 / 2.19
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.376, 152.087, 108.219, 90.00, 90.59, 90.00
R / Rfree (%) 21.2 / 27.6

Other elements in 5uo9:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine also contains other interesting chemical elements:

Magnesium (Mg) 1 atom
Zinc (Zn) 2 atoms
Gadolinium (Gd) 4 atoms
Calcium (Ca) 1 atom
Chlorine (Cl) 5 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-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine (pdb code 5uo9). 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-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine, PDB code: 5uo9:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 5uo9

Go back to Iron Binding Sites List in 5uo9
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) 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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:49.7
occ:1.00
 FE A:HEM501 0.0 49.7 1.0
NC A:HEM501 2.0 52.4 1.0
NB A:HEM501 2.1 54.8 1.0
ND A:HEM501 2.1 41.3 1.0
NA A:HEM501 2.1 52.7 1.0
SG A:CYS184 2.4 48.9 1.0
C1C A:HEM501 3.0 50.0 1.0
C4B A:HEM501 3.0 51.8 1.0
C4C A:HEM501 3.1 49.2 1.0
C1B A:HEM501 3.1 52.1 1.0
C4D A:HEM501 3.1 45.5 1.0
C1D A:HEM501 3.1 49.8 1.0
C1A A:HEM501 3.1 48.8 1.0
C4A A:HEM501 3.2 56.4 1.0
C04 A:8J4503 3.2 84.3 1.0
CB A:CYS184 3.2 53.8 1.0
CHC A:HEM501 3.4 49.8 1.0
CHA A:HEM501 3.5 46.6 1.0
CHD A:HEM501 3.5 50.5 1.0
CHB A:HEM501 3.5 56.8 1.0
C03 A:8J4503 3.5 80.7 1.0
C05 A:8J4503 3.9 88.5 1.0
CA A:CYS184 4.1 45.2 1.0
C3B A:HEM501 4.3 50.6 1.0
C2C A:HEM501 4.3 51.5 1.0
C2B A:HEM501 4.3 49.4 1.0
C3C A:HEM501 4.3 43.2 1.0
C06 A:8J4503 4.4 92.2 1.0
C3D A:HEM501 4.4 49.9 1.0
C2D A:HEM501 4.4 47.2 1.0
C2A A:HEM501 4.4 54.8 1.0
NE1 A:TRP178 4.4 64.3 1.0
C3A A:HEM501 4.4 53.0 1.0
C02 A:8J4503 4.5 82.1 1.0
C10 A:8J4503 4.8 87.6 1.0
C A:CYS184 4.8 43.4 1.0
N A:VAL185 4.9 43.7 1.0
CD1 A:TRP178 4.9 65.2 1.0
N01 A:8J4503 5.0 84.4 1.0

Iron binding site 2 out of 4 in 5uo9

Go back to Iron Binding Sites List in 5uo9
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) 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 Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:34.4
occ:1.00
 FE B:HEM501 0.0 34.4 1.0
NA B:HEM501 2.1 43.4 1.0
ND B:HEM501 2.1 39.2 1.0
NB B:HEM501 2.1 40.6 1.0
NC B:HEM501 2.1 35.7 1.0
SG B:CYS184 2.3 28.0 1.0
C4D B:HEM501 3.1 42.3 1.0
C4A B:HEM501 3.1 40.3 1.0
C1B B:HEM501 3.1 39.0 1.0
C1A B:HEM501 3.1 36.9 1.0
C1D B:HEM501 3.1 36.5 1.0
C04 B:8J4503 3.1 62.3 1.0
C4C B:HEM501 3.1 36.1 1.0
C4B B:HEM501 3.2 41.3 1.0
C1C B:HEM501 3.2 35.8 1.0
CHB B:HEM501 3.4 37.1 1.0
CB B:CYS184 3.4 31.4 1.0
CHD B:HEM501 3.4 34.8 1.0
CHA B:HEM501 3.4 37.1 1.0
C03 B:8J4503 3.5 60.6 1.0
CHC B:HEM501 3.5 32.9 1.0
C05 B:8J4503 3.8 62.0 1.0
CA B:CYS184 4.1 35.3 1.0
C06 B:8J4503 4.2 63.4 1.0
C3A B:HEM501 4.3 34.0 1.0
C3D B:HEM501 4.3 40.8 1.0
C2A B:HEM501 4.3 32.6 1.0
C2B B:HEM501 4.3 42.2 1.0
C2D B:HEM501 4.3 33.9 1.0
NE1 B:TRP178 4.3 33.7 1.0
C3B B:HEM501 4.3 41.8 1.0
C3C B:HEM501 4.4 38.0 1.0
C2C B:HEM501 4.4 38.4 1.0
C02 B:8J4503 4.4 59.0 1.0
C10 B:8J4503 4.6 61.9 1.0
N B:GLY186 4.8 29.9 1.0
N B:VAL185 4.9 31.7 1.0
C B:CYS184 4.9 33.5 1.0
N01 B:8J4503 4.9 62.4 1.0
CD1 B:TRP178 5.0 31.5 1.0

Iron binding site 3 out of 4 in 5uo9

Go back to Iron Binding Sites List in 5uo9
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:47.0
occ:1.00
 FE C:HEM501 0.0 47.0 1.0
NC C:HEM501 2.1 55.4 1.0
NA C:HEM501 2.1 51.1 1.0
ND C:HEM501 2.1 51.7 1.0
NB C:HEM501 2.1 54.6 1.0
SG C:CYS184 2.3 44.2 1.0
C1C C:HEM501 3.1 60.7 1.0
C4D C:HEM501 3.1 56.0 1.0
C1A C:HEM501 3.1 51.8 1.0
C4C C:HEM501 3.1 56.3 1.0
C4A C:HEM501 3.1 49.8 1.0
C4B C:HEM501 3.1 55.0 1.0
C1D C:HEM501 3.1 50.4 1.0
C1B C:HEM501 3.1 53.7 1.0
C04 C:8J4503 3.2 74.5 1.0
CB C:CYS184 3.3 46.8 1.0
CHA C:HEM501 3.4 53.3 1.0
CHC C:HEM501 3.4 59.5 1.0
CHD C:HEM501 3.5 53.1 1.0
CHB C:HEM501 3.5 51.7 1.0
C03 C:8J4503 3.6 74.0 1.0
C05 C:8J4503 4.0 76.8 1.0
CA C:CYS184 4.1 41.2 1.0
C2C C:HEM501 4.3 63.6 1.0
C3C C:HEM501 4.3 59.4 1.0
C3A C:HEM501 4.3 47.7 1.0
C2A C:HEM501 4.3 54.3 1.0
C3D C:HEM501 4.3 51.8 1.0
C3B C:HEM501 4.4 53.0 1.0
C2D C:HEM501 4.4 46.5 1.0
C2B C:HEM501 4.4 54.7 1.0
C06 C:8J4503 4.4 77.7 1.0
C02 C:8J4503 4.4 73.9 1.0
NE1 C:TRP178 4.6 49.0 1.0
C10 C:8J4503 4.8 76.7 1.0
N C:GLY186 4.8 47.9 1.0
C C:CYS184 4.8 40.2 1.0
N C:VAL185 4.9 30.9 1.0
N01 C:8J4503 5.0 76.5 1.0

Iron binding site 4 out of 4 in 5uo9

Go back to Iron Binding Sites List in 5uo9
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-[(3-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-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-Ethyl-5-((Methylamino)Methyl)Phenoxy) Methyl]Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:34.3
occ:1.00
 FE D:HEM501 0.0 34.3 1.0
ND D:HEM501 2.0 40.5 1.0
NA D:HEM501 2.1 47.5 1.0
NC D:HEM501 2.1 45.5 1.0
NB D:HEM501 2.1 34.6 1.0
SG D:CYS184 2.2 30.4 1.0
C04 D:8J4503 3.0 48.0 1.0
C1D D:HEM501 3.0 39.1 1.0
C4C D:HEM501 3.0 41.2 1.0
C4A D:HEM501 3.0 40.6 1.0
C1B D:HEM501 3.1 39.5 1.0
C4D D:HEM501 3.1 46.8 1.0
C1A D:HEM501 3.1 48.2 1.0
C1C D:HEM501 3.2 44.3 1.0
C4B D:HEM501 3.2 37.5 1.0
CHD D:HEM501 3.3 40.4 1.0
CHB D:HEM501 3.4 38.2 1.0
CB D:CYS184 3.4 32.2 1.0
C03 D:8J4503 3.5 51.6 1.0
CHA D:HEM501 3.5 50.9 1.0
CHC D:HEM501 3.6 43.4 1.0
C05 D:8J4503 3.8 53.5 1.0
C06 D:8J4503 4.1 59.4 1.0
CA D:CYS184 4.1 30.6 1.0
C2D D:HEM501 4.2 38.9 1.0
C3A D:HEM501 4.3 43.5 1.0
C3D D:HEM501 4.3 42.6 1.0
C2A D:HEM501 4.3 46.7 1.0
C3C D:HEM501 4.3 42.4 1.0
C2B D:HEM501 4.3 41.8 1.0
C2C D:HEM501 4.4 41.9 1.0
C3B D:HEM501 4.4 38.9 1.0
NE1 D:TRP178 4.5 30.7 1.0
C02 D:8J4503 4.5 50.9 1.0
N D:GLY186 4.8 32.8 1.0
C10 D:8J4503 4.8 57.5 1.0
C D:CYS184 4.8 33.2 1.0
N D:VAL185 4.9 35.2 1.0

Reference:

M.A.Cinelli, H.Li, G.Chreifi, T.L.Poulos, R.B.Silverman. Nitrile in the Hole: Discovery of A Small Auxiliary Pocket in Neuronal Nitric Oxide Synthase Leading to the Development of Potent and Selective 2-Aminoquinoline Inhibitors. J. Med. Chem. V. 60 3958 2017.
ISSN: ISSN 1520-4804
PubMed: 28422508
DOI: 10.1021/ACS.JMEDCHEM.7B00259
Page generated: Tue Aug 6 09:58:36 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy