Iron in PDB 6pp1: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine
Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclopropylmethoxy)Phenyl)-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-(Cyclopropylmethoxy)Phenyl)-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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp1
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)
|
49.71 /
1.76
|
Space group
|
P 1 21 1
|
Cell size a, b, c (Å), α, β, γ (°)
|
59.585,
153.030,
108.781,
90.00,
90.78,
90.00
|
R / Rfree (%)
|
18 /
21.2
|
Other elements in 6pp1:
The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(3-(Aminomethyl)-4-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine also contains other interesting chemical elements:
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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine
(pdb code 6pp1). 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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine, PDB code: 6pp1:
Jump to Iron binding site number:
1;
2;
3;
4;
Iron binding site 1 out
of 4 in 6pp1
Go back to
Iron Binding Sites List in 6pp1
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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_01.jpg) Mono view
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_01_stereo.jpg) 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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
A:Fe501
b:48.9
occ:1.00
|
FE
|
A:HEM501
|
0.0
|
48.9
|
1.0
|
ND
|
A:HEM501
|
2.1
|
47.8
|
1.0
|
NA
|
A:HEM501
|
2.1
|
45.7
|
1.0
|
NC
|
A:HEM501
|
2.1
|
43.5
|
1.0
|
NB
|
A:HEM501
|
2.1
|
47.2
|
1.0
|
SG
|
A:CYS184
|
2.3
|
41.0
|
1.0
|
C4D
|
A:HEM501
|
3.1
|
51.8
|
1.0
|
C1A
|
A:HEM501
|
3.1
|
42.6
|
1.0
|
C1C
|
A:HEM501
|
3.1
|
55.1
|
1.0
|
C4B
|
A:HEM501
|
3.1
|
55.4
|
1.0
|
C1D
|
A:HEM501
|
3.1
|
54.7
|
1.0
|
C4A
|
A:HEM501
|
3.1
|
45.6
|
1.0
|
C1B
|
A:HEM501
|
3.1
|
51.2
|
1.0
|
C4C
|
A:HEM501
|
3.1
|
54.4
|
1.0
|
CHA
|
A:HEM501
|
3.4
|
40.5
|
1.0
|
CHC
|
A:HEM501
|
3.4
|
47.8
|
1.0
|
CB
|
A:CYS184
|
3.4
|
38.0
|
1.0
|
CHB
|
A:HEM501
|
3.5
|
44.9
|
1.0
|
CHD
|
A:HEM501
|
3.5
|
52.9
|
1.0
|
C04
|
A:OU1503
|
3.6
|
66.7
|
1.0
|
C05
|
A:OU1503
|
3.9
|
71.5
|
1.0
|
C11
|
A:OU1503
|
3.9
|
65.4
|
1.0
|
C03
|
A:OU1503
|
4.0
|
57.6
|
1.0
|
CA
|
A:CYS184
|
4.2
|
35.0
|
1.0
|
C3D
|
A:HEM501
|
4.3
|
52.9
|
1.0
|
C06
|
A:OU1503
|
4.3
|
74.3
|
1.0
|
C2D
|
A:HEM501
|
4.3
|
55.9
|
1.0
|
C2A
|
A:HEM501
|
4.3
|
45.1
|
1.0
|
C2B
|
A:HEM501
|
4.3
|
48.6
|
1.0
|
C3B
|
A:HEM501
|
4.3
|
54.4
|
1.0
|
C3A
|
A:HEM501
|
4.3
|
45.0
|
1.0
|
C2C
|
A:HEM501
|
4.3
|
53.9
|
1.0
|
C3C
|
A:HEM501
|
4.3
|
56.6
|
1.0
|
NE1
|
A:TRP178
|
4.3
|
49.7
|
1.0
|
C10
|
A:OU1503
|
4.4
|
65.0
|
1.0
|
C02
|
A:OU1503
|
4.5
|
52.2
|
1.0
|
N01
|
A:OU1503
|
4.7
|
51.7
|
1.0
|
N
|
A:GLY186
|
4.9
|
40.5
|
1.0
|
C
|
A:CYS184
|
5.0
|
41.2
|
1.0
|
CD1
|
A:TRP178
|
5.0
|
48.0
|
1.0
|
|
Iron binding site 2 out
of 4 in 6pp1
Go back to
Iron Binding Sites List in 6pp1
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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_02.jpg) Mono view
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_02_stereo.jpg) 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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
B:Fe502
b:28.2
occ:1.00
|
FE
|
B:HEM502
|
0.0
|
28.2
|
1.0
|
ND
|
B:HEM502
|
2.1
|
31.1
|
1.0
|
NC
|
B:HEM502
|
2.1
|
25.9
|
1.0
|
NA
|
B:HEM502
|
2.1
|
28.0
|
1.0
|
NB
|
B:HEM502
|
2.1
|
33.2
|
1.0
|
SG
|
B:CYS184
|
2.3
|
28.7
|
1.0
|
C1D
|
B:HEM502
|
3.1
|
28.3
|
1.0
|
C1C
|
B:HEM502
|
3.1
|
26.1
|
1.0
|
C1A
|
B:HEM502
|
3.1
|
22.6
|
1.0
|
C4D
|
B:HEM502
|
3.1
|
30.8
|
1.0
|
C4A
|
B:HEM502
|
3.1
|
29.8
|
1.0
|
C4C
|
B:HEM502
|
3.1
|
30.5
|
1.0
|
C1B
|
B:HEM502
|
3.1
|
27.5
|
1.0
|
C4B
|
B:HEM502
|
3.1
|
26.4
|
1.0
|
CB
|
B:CYS184
|
3.4
|
24.6
|
1.0
|
CHA
|
B:HEM502
|
3.4
|
25.9
|
1.0
|
CHD
|
B:HEM502
|
3.5
|
29.1
|
1.0
|
CHC
|
B:HEM502
|
3.5
|
28.9
|
1.0
|
CHB
|
B:HEM502
|
3.5
|
25.7
|
1.0
|
C04
|
B:OU1504
|
3.8
|
36.7
|
1.0
|
C05
|
B:OU1504
|
4.0
|
44.4
|
1.0
|
CA
|
B:CYS184
|
4.1
|
25.0
|
1.0
|
C11
|
B:OU1504
|
4.1
|
35.5
|
1.0
|
C03
|
B:OU1504
|
4.1
|
33.1
|
1.0
|
C2D
|
B:HEM502
|
4.3
|
30.8
|
1.0
|
NE1
|
B:TRP178
|
4.3
|
29.5
|
1.0
|
C3D
|
B:HEM502
|
4.3
|
31.1
|
1.0
|
C2C
|
B:HEM502
|
4.3
|
25.2
|
1.0
|
C2A
|
B:HEM502
|
4.3
|
26.8
|
1.0
|
C3A
|
B:HEM502
|
4.3
|
28.6
|
1.0
|
C3C
|
B:HEM502
|
4.3
|
24.4
|
1.0
|
C2B
|
B:HEM502
|
4.4
|
27.4
|
1.0
|
C3B
|
B:HEM502
|
4.4
|
28.2
|
1.0
|
C06
|
B:OU1504
|
4.4
|
45.4
|
1.0
|
C10
|
B:OU1504
|
4.5
|
46.9
|
1.0
|
C02
|
B:OU1504
|
4.6
|
32.1
|
1.0
|
N01
|
B:OU1504
|
4.8
|
36.4
|
1.0
|
N
|
B:GLY186
|
4.8
|
32.6
|
1.0
|
C
|
B:CYS184
|
4.8
|
26.6
|
1.0
|
CD1
|
B:TRP178
|
4.9
|
27.5
|
1.0
|
N
|
B:VAL185
|
4.9
|
27.9
|
1.0
|
|
Iron binding site 3 out
of 4 in 6pp1
Go back to
Iron Binding Sites List in 6pp1
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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_03.jpg) Mono view
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_03_stereo.jpg) 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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
C:Fe501
b:37.8
occ:1.00
|
FE
|
C:HEM501
|
0.0
|
37.8
|
1.0
|
ND
|
C:HEM501
|
2.1
|
43.9
|
1.0
|
NB
|
C:HEM501
|
2.1
|
42.4
|
1.0
|
NC
|
C:HEM501
|
2.1
|
40.3
|
1.0
|
NA
|
C:HEM501
|
2.1
|
38.7
|
1.0
|
SG
|
C:CYS184
|
2.4
|
38.9
|
1.0
|
C4B
|
C:HEM501
|
3.1
|
43.6
|
1.0
|
C4D
|
C:HEM501
|
3.1
|
42.5
|
1.0
|
C1D
|
C:HEM501
|
3.1
|
45.6
|
1.0
|
C1C
|
C:HEM501
|
3.1
|
43.5
|
1.0
|
C1B
|
C:HEM501
|
3.1
|
38.6
|
1.0
|
C4C
|
C:HEM501
|
3.1
|
42.1
|
1.0
|
C1A
|
C:HEM501
|
3.1
|
41.7
|
1.0
|
C4A
|
C:HEM501
|
3.1
|
36.3
|
1.0
|
CHC
|
C:HEM501
|
3.4
|
40.0
|
1.0
|
CHA
|
C:HEM501
|
3.5
|
33.4
|
1.0
|
CHD
|
C:HEM501
|
3.5
|
46.4
|
1.0
|
CB
|
C:CYS184
|
3.5
|
31.5
|
1.0
|
CHB
|
C:HEM501
|
3.5
|
36.5
|
1.0
|
C04
|
C:OU1503
|
3.8
|
56.4
|
1.0
|
C03
|
C:OU1503
|
4.0
|
50.2
|
1.0
|
C11
|
C:OU1503
|
4.1
|
64.6
|
1.0
|
C05
|
C:OU1503
|
4.1
|
63.3
|
1.0
|
CA
|
C:CYS184
|
4.1
|
34.3
|
1.0
|
C3B
|
C:HEM501
|
4.3
|
42.7
|
1.0
|
C2B
|
C:HEM501
|
4.3
|
38.7
|
1.0
|
C3D
|
C:HEM501
|
4.3
|
43.9
|
1.0
|
C2D
|
C:HEM501
|
4.3
|
42.7
|
1.0
|
C2C
|
C:HEM501
|
4.3
|
44.6
|
1.0
|
C3C
|
C:HEM501
|
4.3
|
41.8
|
1.0
|
C2A
|
C:HEM501
|
4.4
|
45.7
|
1.0
|
C3A
|
C:HEM501
|
4.4
|
39.6
|
1.0
|
NE1
|
C:TRP178
|
4.4
|
39.4
|
1.0
|
C02
|
C:OU1503
|
4.5
|
49.5
|
1.0
|
C10
|
C:OU1503
|
4.6
|
57.3
|
1.0
|
C06
|
C:OU1503
|
4.6
|
66.1
|
1.0
|
N01
|
C:OU1503
|
4.7
|
49.6
|
1.0
|
N
|
C:GLY186
|
4.8
|
36.1
|
1.0
|
C
|
C:CYS184
|
4.9
|
31.2
|
1.0
|
N
|
C:VAL185
|
5.0
|
33.8
|
1.0
|
|
Iron binding site 4 out
of 4 in 6pp1
Go back to
Iron Binding Sites List in 6pp1
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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_04.jpg) Mono view
![](/pictures/FE/pdb/pp/6pp1-FE-sphere_04_stereo.jpg) 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-(Cyclopropylmethoxy)Phenyl)-4- Methylquinolin-2-Amine within 5.0Å range:
probe
|
atom
|
residue
|
distance (Å)
|
B
|
Occ
|
D:Fe502
b:27.6
occ:1.00
|
FE
|
D:HEM502
|
0.0
|
27.6
|
1.0
|
NA
|
D:HEM502
|
2.0
|
26.1
|
1.0
|
ND
|
D:HEM502
|
2.0
|
29.7
|
1.0
|
NC
|
D:HEM502
|
2.1
|
23.9
|
1.0
|
NB
|
D:HEM502
|
2.1
|
28.8
|
1.0
|
SG
|
D:CYS184
|
2.3
|
25.3
|
1.0
|
C1D
|
D:HEM502
|
3.0
|
26.8
|
1.0
|
C4A
|
D:HEM502
|
3.1
|
28.3
|
1.0
|
C1A
|
D:HEM502
|
3.1
|
26.4
|
1.0
|
C4C
|
D:HEM502
|
3.1
|
26.3
|
1.0
|
C1C
|
D:HEM502
|
3.1
|
26.5
|
1.0
|
C4D
|
D:HEM502
|
3.1
|
23.0
|
1.0
|
C1B
|
D:HEM502
|
3.1
|
29.8
|
1.0
|
C4B
|
D:HEM502
|
3.1
|
25.0
|
1.0
|
CB
|
D:CYS184
|
3.3
|
26.6
|
1.0
|
CHD
|
D:HEM502
|
3.4
|
27.1
|
1.0
|
CHB
|
D:HEM502
|
3.4
|
27.6
|
1.0
|
CHC
|
D:HEM502
|
3.5
|
27.0
|
1.0
|
CHA
|
D:HEM502
|
3.5
|
24.0
|
1.0
|
C04
|
D:OU1504
|
3.9
|
37.5
|
1.0
|
C05
|
D:OU1504
|
4.0
|
35.6
|
1.0
|
CA
|
D:CYS184
|
4.1
|
23.5
|
1.0
|
C11
|
D:OU1504
|
4.2
|
38.8
|
1.0
|
C03
|
D:OU1504
|
4.2
|
35.7
|
1.0
|
C2D
|
D:HEM502
|
4.3
|
28.7
|
1.0
|
C3A
|
D:HEM502
|
4.3
|
28.2
|
1.0
|
C2A
|
D:HEM502
|
4.3
|
26.5
|
1.0
|
C3D
|
D:HEM502
|
4.3
|
30.5
|
1.0
|
C3C
|
D:HEM502
|
4.3
|
25.9
|
1.0
|
C06
|
D:OU1504
|
4.3
|
39.5
|
1.0
|
C2C
|
D:HEM502
|
4.3
|
28.7
|
1.0
|
C2B
|
D:HEM502
|
4.3
|
27.7
|
1.0
|
NE1
|
D:TRP178
|
4.4
|
28.6
|
1.0
|
C3B
|
D:HEM502
|
4.4
|
29.3
|
1.0
|
C10
|
D:OU1504
|
4.4
|
38.5
|
1.0
|
C02
|
D:OU1504
|
4.6
|
34.0
|
1.0
|
N01
|
D:OU1504
|
4.7
|
36.6
|
1.0
|
N
|
D:GLY186
|
4.8
|
28.2
|
1.0
|
C
|
D:CYS184
|
4.8
|
26.4
|
1.0
|
CD1
|
D:TRP178
|
5.0
|
28.0
|
1.0
|
C07
|
D:OU1504
|
5.0
|
44.2
|
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: Wed Aug 7 06:24:03 2024
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