Iron in PDB 8uft: Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine

Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine

All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine, PDB code: 8uft 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) 40.02 / 1.78
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 60.06, 154.607, 108.575, 90, 90.73, 90
R / Rfree (%) 17.5 / 21

Other elements in 8uft:

The structure of Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine also contains other interesting chemical elements:

Gadolinium (Gd) 4 atoms
Chlorine (Cl) 4 atoms
Zinc (Zn) 2 atoms
Calcium (Ca) 3 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine (pdb code 8uft). 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 P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine, PDB code: 8uft:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in 8uft

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Iron binding site 1 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)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 P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:29.2
occ:1.00
 FE A:HEM501 0.0 29.2 1.0
ND A:HEM501 2.1 26.6 1.0
NA A:HEM501 2.1 28.7 1.0
NB A:HEM501 2.1 30.3 1.0
NC A:HEM501 2.1 34.3 1.0
SG A:CYS184 2.4 25.4 1.0
C1D A:HEM501 3.1 27.9 1.0
C4D A:HEM501 3.1 26.8 1.0
C4A A:HEM501 3.1 28.0 1.0
C1B A:HEM501 3.1 29.3 1.0
C4B A:HEM501 3.1 30.5 1.0
C1C A:HEM501 3.1 33.8 1.0
C1A A:HEM501 3.1 29.0 1.0
C4C A:HEM501 3.1 35.0 1.0
CB A:CYS184 3.4 24.9 1.0
CHB A:HEM501 3.5 31.7 1.0
CHA A:HEM501 3.5 23.2 1.0
CHD A:HEM501 3.5 30.1 1.0
CHC A:HEM501 3.5 32.7 1.0
C04 A:WK2503 3.7 37.6 1.0
C03 A:WK2503 3.9 35.0 1.0
C11 A:WK2503 4.0 40.4 1.0
C05 A:WK2503 4.1 36.9 1.0
CA A:CYS184 4.1 25.1 1.0
C2D A:HEM501 4.3 31.2 1.0
C3D A:HEM501 4.3 28.8 1.0
C3A A:HEM501 4.3 33.6 1.0
C2B A:HEM501 4.3 32.1 1.0
C3B A:HEM501 4.3 32.0 1.0
C2A A:HEM501 4.3 32.7 1.0
C2C A:HEM501 4.3 36.0 1.0
C3C A:HEM501 4.3 37.5 1.0
NE1 A:TRP178 4.4 27.4 1.0
C02 A:WK2503 4.4 36.0 1.0
C06 A:WK2503 4.6 38.9 1.0
C10 A:WK2503 4.6 42.6 1.0
N01 A:WK2503 4.7 35.6 1.0
C A:CYS184 4.8 25.3 1.0
N A:GLY186 4.8 28.1 1.0
N A:VAL185 5.0 25.9 1.0

Iron binding site 2 out of 4 in 8uft

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Iron binding site 2 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)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 P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe502

b:16.2
occ:1.00
 FE B:HEM502 0.0 16.2 1.0
NA B:HEM502 2.0 16.0 1.0
NB B:HEM502 2.1 20.3 1.0
ND B:HEM502 2.1 21.9 1.0
NC B:HEM502 2.1 19.8 1.0
SG B:CYS184 2.3 19.3 1.0
C4A B:HEM502 3.0 20.9 1.0
C1B B:HEM502 3.1 23.2 1.0
C1D B:HEM502 3.1 18.6 1.0
C1A B:HEM502 3.1 19.6 1.0
C4C B:HEM502 3.1 23.9 1.0
C1C B:HEM502 3.1 20.6 1.0
C4D B:HEM502 3.1 21.5 1.0
C4B B:HEM502 3.1 20.2 1.0
CB B:CYS184 3.3 15.8 1.0
CHB B:HEM502 3.4 19.4 1.0
CHD B:HEM502 3.4 21.5 1.0
CHA B:HEM502 3.5 16.2 1.0
CHC B:HEM502 3.5 19.0 1.0
C04 B:WK2504 3.7 24.4 1.0
C03 B:WK2504 4.0 19.3 1.0
C11 B:WK2504 4.0 25.1 1.0
CA B:CYS184 4.0 17.4 1.0
C05 B:WK2504 4.1 26.2 1.0
C3A B:HEM502 4.3 21.4 1.0
C2A B:HEM502 4.3 25.5 1.0
C2D B:HEM502 4.3 20.3 1.0
C2B B:HEM502 4.3 22.3 1.0
C3D B:HEM502 4.3 21.2 1.0
C3C B:HEM502 4.3 17.8 1.0
C2C B:HEM502 4.3 19.8 1.0
NE1 B:TRP178 4.3 18.9 1.0
C3B B:HEM502 4.3 23.9 1.0
C02 B:WK2504 4.5 19.7 1.0
C06 B:WK2504 4.6 27.3 1.0
C10 B:WK2504 4.6 26.9 1.0
N01 B:WK2504 4.7 22.4 1.0
N B:GLY186 4.8 20.2 1.0
C B:CYS184 4.8 22.7 1.0
N B:VAL185 5.0 19.1 1.0
CD1 B:TRP178 5.0 18.2 1.0

Iron binding site 3 out of 4 in 8uft

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Iron binding site 3 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)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 P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:25.5
occ:1.00
 FE C:HEM501 0.0 25.5 1.0
NA C:HEM501 2.0 30.8 1.0
ND C:HEM501 2.1 31.4 1.0
NB C:HEM501 2.1 35.5 1.0
NC C:HEM501 2.1 35.4 1.0
SG C:CYS184 2.3 27.1 1.0
C1A C:HEM501 3.0 33.9 1.0
C4D C:HEM501 3.0 35.2 1.0
C4A C:HEM501 3.1 29.5 1.0
C1D C:HEM501 3.1 37.0 1.0
C1B C:HEM501 3.1 34.7 1.0
C4B C:HEM501 3.1 34.8 1.0
C4C C:HEM501 3.1 36.6 1.0
C1C C:HEM501 3.1 34.4 1.0
CB C:CYS184 3.3 26.5 1.0
CHA C:HEM501 3.4 34.6 1.0
CHB C:HEM501 3.4 30.1 1.0
CHD C:HEM501 3.5 34.4 1.0
CHC C:HEM501 3.5 34.4 1.0
C04 C:WK2503 3.7 45.0 1.0
C11 C:WK2503 3.9 49.5 1.0
C03 C:WK2503 3.9 41.7 1.0
C05 C:WK2503 4.0 41.4 1.0
CA C:CYS184 4.1 25.4 1.0
C2A C:HEM501 4.3 33.1 1.0
C3D C:HEM501 4.3 41.2 1.0
C3A C:HEM501 4.3 33.8 1.0
C2D C:HEM501 4.3 39.1 1.0
C2B C:HEM501 4.3 35.9 1.0
C3B C:HEM501 4.3 35.8 1.0
C3C C:HEM501 4.4 37.2 1.0
C2C C:HEM501 4.4 33.1 1.0
NE1 C:TRP178 4.4 29.0 1.0
C02 C:WK2503 4.5 36.0 1.0
C06 C:WK2503 4.5 44.3 1.0
C10 C:WK2503 4.6 37.6 1.0
N01 C:WK2503 4.8 33.7 1.0
N C:GLY186 4.9 31.2 1.0
C C:CYS184 4.9 29.6 1.0

Iron binding site 4 out of 4 in 8uft

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Iron binding site 4 out of 4 in the Structure of Human Endothelial Nitric Oxide Synthase P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)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 P370N Mutant Heme Domain in Complex with 4-Methyl-7-(4-Methyl-2,3,4,5- Tetrahydrobenzo[F][1,4]Oxazepin-7-Yl)Quinolin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:20.1
occ:1.00
 FE D:HEM501 0.0 20.1 1.0
NA D:HEM501 2.0 23.7 1.0
ND D:HEM501 2.1 18.6 1.0
NC D:HEM501 2.1 20.3 1.0
NB D:HEM501 2.1 20.9 1.0
SG D:CYS184 2.4 17.1 1.0
C4A D:HEM501 3.1 20.1 1.0
C1A D:HEM501 3.1 21.1 1.0
C1D D:HEM501 3.1 21.1 1.0
C4D D:HEM501 3.1 19.0 1.0
C1C D:HEM501 3.1 20.0 1.0
C4C D:HEM501 3.1 21.8 1.0
C1B D:HEM501 3.1 17.2 1.0
C4B D:HEM501 3.1 18.3 1.0
CB D:CYS184 3.3 15.8 1.0
CHB D:HEM501 3.4 17.7 1.0
CHA D:HEM501 3.4 18.5 1.0
CHD D:HEM501 3.5 20.5 1.0
CHC D:HEM501 3.5 19.4 1.0
C04 D:WK2503 3.7 27.1 1.0
C11 D:WK2503 4.0 29.8 1.0
C03 D:WK2503 4.0 23.9 1.0
C05 D:WK2503 4.1 28.9 1.0
CA D:CYS184 4.1 19.9 1.0
C2A D:HEM501 4.3 24.7 1.0
C3A D:HEM501 4.3 20.9 1.0
C3D D:HEM501 4.3 20.8 1.0
C2D D:HEM501 4.3 21.4 1.0
C2C D:HEM501 4.3 20.4 1.0
C2B D:HEM501 4.3 17.7 1.0
C3C D:HEM501 4.3 20.4 1.0
C3B D:HEM501 4.3 16.9 1.0
NE1 D:TRP178 4.4 19.1 1.0
C02 D:WK2503 4.5 23.1 1.0
C06 D:WK2503 4.5 30.9 1.0
C10 D:WK2503 4.6 26.9 1.0
N01 D:WK2503 4.7 21.7 1.0
N D:GLY186 4.8 17.9 1.0
C D:CYS184 4.9 19.9 1.0
CD1 D:TRP178 5.0 21.6 1.0
N D:VAL185 5.0 20.2 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 18:31:59 2024

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