Iron in PDB 8ufr: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride, PDB code: 8ufr 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) 39.12 / 1.87
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.491, 152.859, 108.942, 90, 90.86, 90
R / Rfree (%) 20.7 / 25.1

Other elements in 8ufr:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride 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 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride (pdb code 8ufr). 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 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride, PDB code: 8ufr:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8ufr

Go back to Iron Binding Sites List in 8ufr
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


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 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:49.6
occ:1.00
 FE A:HEM501 0.0 49.6 1.0
NC A:HEM501 2.1 63.9 1.0
NA A:HEM501 2.1 57.7 1.0
ND A:HEM501 2.1 58.1 1.0
NB A:HEM501 2.1 56.8 1.0
SG A:CYS184 2.3 49.1 1.0
C4C A:HEM501 3.1 68.2 1.0
C1D A:HEM501 3.1 68.6 1.0
C1C A:HEM501 3.1 59.2 1.0
C4A A:HEM501 3.1 56.9 1.0
C1B A:HEM501 3.1 64.7 1.0
C1A A:HEM501 3.1 53.3 1.0
C4D A:HEM501 3.1 61.0 1.0
C4B A:HEM501 3.1 59.6 1.0
CHD A:HEM501 3.4 72.9 1.0
CHB A:HEM501 3.4 65.7 1.0
CHC A:HEM501 3.4 53.3 1.0
CHA A:HEM501 3.5 51.1 1.0
CB A:CYS184 3.5 52.4 1.0
C04 A:WK2503 3.6 63.5 1.0
C11 A:WK2503 3.8 68.6 1.0
C03 A:WK2503 3.8 52.1 1.0
C05 A:WK2503 4.0 67.3 1.0
CA A:CYS184 4.2 43.4 1.0
C3C A:HEM501 4.3 70.0 1.0
C2C A:HEM501 4.3 67.4 1.0
C2D A:HEM501 4.3 64.0 1.0
C3A A:HEM501 4.3 50.0 1.0
C2B A:HEM501 4.3 54.7 1.0
C2A A:HEM501 4.3 56.5 1.0
C3D A:HEM501 4.3 65.0 1.0
C3B A:HEM501 4.3 59.9 1.0
C02 A:WK2503 4.4 49.7 1.0
C06 A:WK2503 4.5 70.4 1.0
NE1 A:TRP178 4.5 56.4 1.0
C10 A:WK2503 4.6 63.9 1.0
N01 A:WK2503 4.7 54.1 1.0
C A:CYS184 5.0 37.6 1.0

Iron binding site 2 out of 4 in 8ufr

Go back to Iron Binding Sites List in 8ufr
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


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 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride 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 2.0 37.6 1.0
ND B:HEM501 2.1 32.8 1.0
NB B:HEM501 2.1 32.9 1.0
NC B:HEM501 2.2 27.9 1.0
SG B:CYS184 2.3 28.3 1.0
C4A B:HEM501 3.0 34.3 1.0
C4D B:HEM501 3.0 32.2 1.0
C1A B:HEM501 3.0 30.1 1.0
C1B B:HEM501 3.1 27.7 1.0
C1D B:HEM501 3.1 27.7 1.0
C4B B:HEM501 3.2 35.9 1.0
C4C B:HEM501 3.2 34.2 1.0
C1C B:HEM501 3.2 32.2 1.0
CHB B:HEM501 3.4 29.7 1.0
CB B:CYS184 3.4 33.8 1.0
CHA B:HEM501 3.4 27.1 1.0
CHD B:HEM501 3.5 32.8 1.0
CHC B:HEM501 3.5 28.8 1.0
C04 B:WK2503 3.8 38.6 1.0
C11 B:WK2503 4.0 40.3 1.0
C03 B:WK2503 4.0 30.1 1.0
CA B:CYS184 4.1 35.0 1.0
C05 B:WK2503 4.1 39.6 1.0
C3D B:HEM501 4.2 33.7 1.0
C3A B:HEM501 4.3 34.5 1.0
C2A B:HEM501 4.3 37.3 1.0
C2D B:HEM501 4.3 32.9 1.0
C2B B:HEM501 4.3 36.0 1.0
C3B B:HEM501 4.3 33.8 1.0
NE1 B:TRP178 4.4 34.4 1.0
C3C B:HEM501 4.4 33.6 1.0
C2C B:HEM501 4.4 31.0 1.0
C06 B:WK2503 4.5 41.0 1.0
C02 B:WK2503 4.5 30.9 1.0
C10 B:WK2503 4.6 38.1 1.0
N01 B:WK2503 4.8 37.2 1.0
N B:GLY186 4.8 39.2 1.0
C B:CYS184 4.8 33.3 1.0
N B:VAL185 5.0 33.2 1.0

Iron binding site 3 out of 4 in 8ufr

Go back to Iron Binding Sites List in 8ufr
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


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 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:41.0
occ:1.00
 FE C:HEM501 0.0 41.0 1.0
ND C:HEM501 2.0 47.3 1.0
NC C:HEM501 2.1 51.6 1.0
NB C:HEM501 2.1 43.6 1.0
NA C:HEM501 2.1 44.6 1.0
SG C:CYS184 2.3 37.5 1.0
C4D C:HEM501 3.0 47.0 1.0
C1C C:HEM501 3.1 49.5 1.0
C1D C:HEM501 3.1 51.4 1.0
C4B C:HEM501 3.1 45.3 1.0
C1A C:HEM501 3.1 37.2 1.0
C1B C:HEM501 3.1 42.7 1.0
C4C C:HEM501 3.1 50.7 1.0
C4A C:HEM501 3.2 43.2 1.0
CB C:CYS184 3.3 42.0 1.0
CHC C:HEM501 3.4 38.0 1.0
CHA C:HEM501 3.4 36.5 1.0
CHD C:HEM501 3.5 44.8 1.0
CHB C:HEM501 3.5 38.5 1.0
C04 C:WK2503 3.9 63.8 1.0
C03 C:WK2503 4.0 50.4 1.0
CA C:CYS184 4.1 39.4 1.0
C11 C:WK2503 4.1 67.5 1.0
C3D C:HEM501 4.2 50.8 1.0
C05 C:WK2503 4.2 67.6 1.0
C2D C:HEM501 4.3 41.9 1.0
C3B C:HEM501 4.3 44.6 1.0
C2C C:HEM501 4.3 55.3 1.0
C2B C:HEM501 4.3 43.0 1.0
C3C C:HEM501 4.4 52.2 1.0
C2A C:HEM501 4.4 52.0 1.0
C3A C:HEM501 4.4 46.0 1.0
NE1 C:TRP178 4.4 47.9 1.0
C02 C:WK2503 4.5 51.2 1.0
N C:GLY186 4.7 45.7 1.0
C10 C:WK2503 4.7 57.5 1.0
C06 C:WK2503 4.7 69.4 1.0
C C:CYS184 4.8 34.1 1.0
N01 C:WK2503 4.8 53.3 1.0
N C:VAL185 4.9 35.7 1.0
CD1 C:TRP178 5.0 44.0 1.0

Iron binding site 4 out of 4 in 8ufr

Go back to Iron Binding Sites List in 8ufr
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride


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 4-Methyl-7-(4-Methyl-2,3,4,5-Tetrahydrobenzo[F][1, 4]Oxazepin-7-Yl)Quinolin-2-Amine Dihydrochloride within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:30.2
occ:1.00
 FE D:HEM501 0.0 30.2 1.0
ND D:HEM501 2.0 34.8 1.0
NA D:HEM501 2.1 27.8 1.0
NB D:HEM501 2.1 23.0 1.0
NC D:HEM501 2.2 26.3 1.0
SG D:CYS184 2.2 26.6 1.0
C1D D:HEM501 3.0 32.6 1.0
C4A D:HEM501 3.0 34.2 1.0
C4D D:HEM501 3.1 30.6 1.0
C1B D:HEM501 3.1 31.0 1.0
C1A D:HEM501 3.1 22.8 1.0
C4C D:HEM501 3.1 29.9 1.0
C1C D:HEM501 3.2 25.6 1.0
C4B D:HEM501 3.2 23.6 1.0
CB D:CYS184 3.3 33.4 1.0
CHB D:HEM501 3.3 29.7 1.0
CHD D:HEM501 3.4 28.3 1.0
CHA D:HEM501 3.5 21.5 1.0
CHC D:HEM501 3.6 25.1 1.0
C04 D:WK2503 3.8 35.7 1.0
CA D:CYS184 4.0 25.7 1.0
C11 D:WK2503 4.1 34.0 1.0
C03 D:WK2503 4.1 34.6 1.0
C05 D:WK2503 4.1 38.0 1.0
C3D D:HEM501 4.2 35.8 1.0
C2D D:HEM501 4.2 34.9 1.0
C3A D:HEM501 4.3 30.8 1.0
C2A D:HEM501 4.3 34.7 1.0
C2B D:HEM501 4.3 31.6 1.0
C3C D:HEM501 4.4 33.8 1.0
C3B D:HEM501 4.4 35.2 1.0
C2C D:HEM501 4.4 30.1 1.0
NE1 D:TRP178 4.4 34.9 1.0
C06 D:WK2503 4.5 41.6 1.0
C02 D:WK2503 4.6 34.1 1.0
C10 D:WK2503 4.6 39.1 1.0
N D:GLY186 4.7 31.4 1.0
N01 D:WK2503 4.8 34.3 1.0
C D:CYS184 4.8 32.9 1.0

Reference:

H.Li, C.D.Hardy, C.T.Reidl, Q.Jing, F.Xue, M.Cinelli, R.B.Silverman, T.L.Poulos. Crystallographic and Computational Insights Into Isoform-Selective Dynamics in Nitric Oxide Synthase. Biochemistry 2024.
ISSN: ISSN 0006-2960
PubMed: 38417024
DOI: 10.1021/ACS.BIOCHEM.3C00601
Page generated: Sat Aug 10 18:30:21 2024

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