Iron in PDB 8ufu: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine, PDB code: 8ufu 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) 38.74 / 2.05
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 59.673, 152.827, 109.162, 90, 90.82, 90
R / Rfree (%) 20.5 / 25.6

Other elements in 8ufu:

The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine also contains other interesting chemical elements:

Zinc (Zn) 6 atoms
Calcium (Ca) 2 atoms
Chlorine (Cl) 4 atoms
Gadolinium (Gd) 2 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine (pdb code 8ufu). 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine, PDB code: 8ufu:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8ufu

Go back to Iron Binding Sites List in 8ufu
Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:50.9
occ:1.00
 FE A:HEM501 0.0 50.9 1.0
ND A:HEM501 2.0 58.4 1.0
NB A:HEM501 2.1 61.1 1.0
NA A:HEM501 2.1 56.5 1.0
NC A:HEM501 2.1 61.3 1.0
SG A:CYS184 2.3 41.8 1.0
C4D A:HEM501 3.0 58.1 1.0
C1D A:HEM501 3.0 69.6 1.0
C1B A:HEM501 3.1 66.6 1.0
C1A A:HEM501 3.1 55.4 1.0
C4B A:HEM501 3.1 66.3 1.0
C4A A:HEM501 3.1 60.5 1.0
C4C A:HEM501 3.1 67.0 1.0
C1C A:HEM501 3.1 65.9 1.0
CB A:CYS184 3.4 44.6 1.0
CHA A:HEM501 3.4 55.9 1.0
CHD A:HEM501 3.5 68.5 1.0
C04 A:WRI502 3.5 74.8 1.0
CHB A:HEM501 3.5 58.0 1.0
CHC A:HEM501 3.5 71.7 1.0
C11 A:WRI502 3.6 80.6 1.0
C03 A:WRI502 3.7 64.6 1.0
C05 A:WRI502 3.9 75.8 1.0
CA A:CYS184 4.1 47.0 1.0
C3D A:HEM501 4.2 70.1 1.0
C2D A:HEM501 4.2 70.3 1.0
C2B A:HEM501 4.3 62.4 1.0
C06 A:WRI502 4.3 76.4 1.0
C3B A:HEM501 4.3 56.8 1.0
C3A A:HEM501 4.3 59.8 1.0
C2A A:HEM501 4.3 62.6 1.0
C3C A:HEM501 4.3 71.4 1.0
C2C A:HEM501 4.4 69.0 1.0
C02 A:WRI502 4.4 66.7 1.0
C10 A:WRI502 4.5 73.7 1.0
NE1 A:TRP178 4.6 59.9 1.0
N01 A:WRI502 4.7 70.4 1.0
C A:CYS184 5.0 43.3 1.0
N A:GLY186 5.0 46.8 1.0

Iron binding site 2 out of 4 in 8ufu

Go back to Iron Binding Sites List in 8ufu
Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:34.7
occ:1.00
 FE B:HEM501 0.0 34.7 1.0
ND B:HEM501 2.1 43.2 1.0
NA B:HEM501 2.1 43.9 1.0
NB B:HEM501 2.1 36.4 1.0
NC B:HEM501 2.1 38.9 1.0
SG B:CYS184 2.3 29.3 1.0
C1D B:HEM501 3.0 39.6 1.0
C4A B:HEM501 3.1 41.8 1.0
C1B B:HEM501 3.1 35.6 1.0
C4D B:HEM501 3.1 46.3 1.0
C4C B:HEM501 3.1 40.1 1.0
C1A B:HEM501 3.1 42.3 1.0
C4B B:HEM501 3.2 42.9 1.0
C1C B:HEM501 3.2 39.0 1.0
CB B:CYS184 3.3 30.7 1.0
CHB B:HEM501 3.4 31.2 1.0
CHD B:HEM501 3.4 33.6 1.0
CHA B:HEM501 3.5 41.2 1.0
CHC B:HEM501 3.6 36.1 1.0
C04 B:WRI502 3.6 56.4 1.0
C11 B:WRI502 3.8 53.3 1.0
C05 B:WRI502 4.0 46.2 1.0
C03 B:WRI502 4.0 43.6 1.0
CA B:CYS184 4.1 34.3 1.0
C2D B:HEM501 4.3 45.0 1.0
C3D B:HEM501 4.3 45.2 1.0
C2B B:HEM501 4.3 40.0 1.0
C3A B:HEM501 4.3 37.5 1.0
C2A B:HEM501 4.3 48.6 1.0
C06 B:WRI502 4.3 53.1 1.0
C3B B:HEM501 4.4 41.5 1.0
C3C B:HEM501 4.4 48.8 1.0
NE1 B:TRP178 4.4 33.5 1.0
C2C B:HEM501 4.4 39.9 1.0
C02 B:WRI502 4.6 44.6 1.0
C10 B:WRI502 4.6 45.8 1.0
N01 B:WRI502 4.8 44.3 1.0
C B:CYS184 4.8 32.4 1.0
N B:GLY186 4.9 33.5 1.0
N B:VAL185 4.9 32.3 1.0

Iron binding site 3 out of 4 in 8ufu

Go back to Iron Binding Sites List in 8ufu
Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:40.3
occ:1.00
 FE C:HEM501 0.0 40.3 1.0
NB C:HEM501 2.1 50.0 1.0
ND C:HEM501 2.1 42.7 1.0
NA C:HEM501 2.1 50.6 1.0
NC C:HEM501 2.1 44.5 1.0
SG C:CYS184 2.3 39.7 1.0
C4B C:HEM501 3.0 45.6 1.0
C4D C:HEM501 3.0 49.5 1.0
C1A C:HEM501 3.1 46.3 1.0
C1C C:HEM501 3.1 55.5 1.0
C1B C:HEM501 3.1 50.7 1.0
C4A C:HEM501 3.1 48.6 1.0
C1D C:HEM501 3.1 52.6 1.0
C4C C:HEM501 3.2 45.3 1.0
CB C:CYS184 3.2 42.6 1.0
CHC C:HEM501 3.4 47.2 1.0
CHA C:HEM501 3.4 40.7 1.0
CHB C:HEM501 3.5 45.6 1.0
CHD C:HEM501 3.5 47.5 1.0
C04 C:WRI502 3.7 61.7 1.0
C11 C:WRI502 3.9 63.2 1.0
C03 C:WRI502 4.0 55.0 1.0
CA C:CYS184 4.0 31.7 1.0
C05 C:WRI502 4.0 60.7 1.0
C3B C:HEM501 4.2 53.3 1.0
C3D C:HEM501 4.3 52.0 1.0
C2B C:HEM501 4.3 49.5 1.0
C2D C:HEM501 4.3 48.5 1.0
C2A C:HEM501 4.3 55.0 1.0
C3A C:HEM501 4.3 48.2 1.0
C2C C:HEM501 4.4 57.3 1.0
C3C C:HEM501 4.4 47.8 1.0
NE1 C:TRP178 4.4 53.4 1.0
C06 C:WRI502 4.5 61.8 1.0
C02 C:WRI502 4.5 57.4 1.0
C10 C:WRI502 4.6 62.0 1.0
N01 C:WRI502 4.8 64.8 1.0
C C:CYS184 4.8 37.4 1.0
N C:GLY186 4.9 43.4 1.0
N C:VAL185 5.0 34.1 1.0

Iron binding site 4 out of 4 in 8ufu

Go back to Iron Binding Sites List in 8ufu
Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with 7-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 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-(9-Amino-6,7,8,9-Tetrahydro-5H-Benzo[7]Annulen-2-Yl)- 4-Methylquinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:32.6
occ:1.00
 FE D:HEM501 0.0 32.6 1.0
ND D:HEM501 2.0 36.5 1.0
NA D:HEM501 2.1 38.3 1.0
NC D:HEM501 2.1 36.0 1.0
NB D:HEM501 2.1 38.2 1.0
SG D:CYS184 2.3 28.9 1.0
C1D D:HEM501 3.0 37.2 1.0
C4D D:HEM501 3.1 38.9 1.0
C4C D:HEM501 3.1 31.6 1.0
C1B D:HEM501 3.1 37.1 1.0
C4A D:HEM501 3.1 39.8 1.0
C1A D:HEM501 3.1 36.8 1.0
C1C D:HEM501 3.1 38.9 1.0
C4B D:HEM501 3.2 39.3 1.0
CB D:CYS184 3.3 35.1 1.0
CHD D:HEM501 3.4 26.6 1.0
CHB D:HEM501 3.4 28.4 1.0
CHA D:HEM501 3.5 33.5 1.0
CHC D:HEM501 3.5 38.3 1.0
C04 D:WRI502 3.7 48.8 1.0
C11 D:WRI502 3.9 51.5 1.0
C05 D:WRI502 4.0 46.7 1.0
C03 D:WRI502 4.0 46.8 1.0
CA D:CYS184 4.1 31.3 1.0
C2D D:HEM501 4.2 41.7 1.0
C3D D:HEM501 4.2 44.6 1.0
C3C D:HEM501 4.3 45.8 1.0
C2B D:HEM501 4.3 48.0 1.0
C3A D:HEM501 4.3 42.4 1.0
C2C D:HEM501 4.3 39.8 1.0
C2A D:HEM501 4.3 40.6 1.0
C3B D:HEM501 4.4 44.7 1.0
NE1 D:TRP178 4.4 40.7 1.0
C06 D:WRI502 4.4 55.4 1.0
C02 D:WRI502 4.6 39.7 1.0
C10 D:WRI502 4.6 52.6 1.0
N01 D:WRI502 4.8 45.6 1.0
C D:CYS184 4.8 33.6 1.0
N D:GLY186 4.9 29.2 1.0
N D:VAL185 4.9 34.8 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 18:36:50 2024

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