Atomistry » Iron » PDB 8u7y-8vtm » 8ufu
Atomistry »
  Iron »
    PDB 8u7y-8vtm »
      8ufu »

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

Last articles

Mg in 4Y52
Mg in 4Y30
Mg in 4Y2V
Mg in 4Y2X
Mg in 4Y2Y
Mg in 4Y2U
Mg in 4Y2T
Mg in 4Y2Q
Mg in 4Y2R
Mg in 4Y2S
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy