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Iron in PDB 4k5h: Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine

Enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine

All present enzymatic activity of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine, PDB code: 4k5h was solved by G.Chreifi, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 42.72 / 2.25
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 57.911, 106.430, 156.899, 90.00, 90.00, 90.00
R / Rfree (%) 15.5 / 20.6

Other elements in 4k5h:

The structure of Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine also contains other interesting chemical elements:

Arsenic (As) 2 atoms
Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine (pdb code 4k5h). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine, PDB code: 4k5h:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 4k5h

Go back to Iron Binding Sites List in 4k5h
Iron binding site 1 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-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 Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:28.0
occ:1.00
FE A:HEM501 0.0 28.0 1.0
ND A:HEM501 1.9 26.9 1.0
NA A:HEM501 2.0 28.9 1.0
NB A:HEM501 2.0 25.5 1.0
NC A:HEM501 2.0 28.4 1.0
SG A:CYS186 2.4 27.7 1.0
C1D A:HEM501 2.9 29.1 1.0
C4D A:HEM501 2.9 26.9 1.0
C1B A:HEM501 2.9 26.6 1.0
C4B A:HEM501 3.0 29.9 1.0
C1A A:HEM501 3.0 28.4 1.0
C4C A:HEM501 3.0 31.4 1.0
C1C A:HEM501 3.0 28.8 1.0
C4A A:HEM501 3.0 27.6 1.0
CHA A:HEM501 3.4 26.9 1.0
CHB A:HEM501 3.4 27.8 1.0
CHD A:HEM501 3.4 30.7 1.0
CHC A:HEM501 3.4 28.1 1.0
CB A:CYS186 3.4 28.2 1.0
C23 A:1Q6503 3.8 32.3 1.0
C24 A:1Q6503 3.9 31.4 1.0
C27 A:1Q6503 4.1 32.3 1.0
C2B A:HEM501 4.2 27.7 1.0
CA A:CYS186 4.2 26.4 1.0
C2D A:HEM501 4.2 25.8 1.0
C2A A:HEM501 4.2 28.9 1.0
C3D A:HEM501 4.2 25.3 1.0
C3C A:HEM501 4.2 30.4 1.0
C2C A:HEM501 4.2 30.9 1.0
C3A A:HEM501 4.2 27.3 1.0
C3B A:HEM501 4.3 27.9 1.0
NE1 A:TRP180 4.4 26.0 1.0
C22 A:1Q6503 4.4 30.1 1.0
C25 A:1Q6503 4.6 32.2 1.0
N A:GLY188 4.9 28.8 1.0
N22 A:1Q6503 5.0 30.7 1.0
N21 A:1Q6503 5.0 28.7 1.0

Iron binding site 2 out of 2 in 4k5h

Go back to Iron Binding Sites List in 4k5h
Iron binding site 2 out of 2 in the Structure of Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-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 Bovine Endothelial Nitric Oxide Synthase Heme Domain in Complex with (S)-1,2-Bis((2-Amino-4-Methylpyridin-6-Yl)-Methoxy)- Propan-3-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:30.8
occ:1.00
FE B:HEM501 0.0 30.8 1.0
ND B:HEM501 1.9 29.7 1.0
NA B:HEM501 2.0 30.1 1.0
NC B:HEM501 2.1 28.5 1.0
NB B:HEM501 2.1 26.5 1.0
SG B:CYS186 2.3 31.4 1.0
C1D B:HEM501 3.0 29.2 1.0
C4D B:HEM501 3.0 26.9 1.0
C4A B:HEM501 3.0 28.3 1.0
C1A B:HEM501 3.0 28.5 1.0
C1B B:HEM501 3.0 29.0 1.0
C4C B:HEM501 3.0 30.1 1.0
C4B B:HEM501 3.0 31.2 1.0
C1C B:HEM501 3.1 31.5 1.0
CHB B:HEM501 3.4 29.3 1.0
CHA B:HEM501 3.4 26.3 1.0
CHD B:HEM501 3.4 30.6 1.0
CHC B:HEM501 3.4 32.8 1.0
CB B:CYS186 3.4 32.2 1.0
C23 B:1Q6503 3.9 37.6 1.0
C24 B:1Q6503 4.0 37.6 1.0
C27 B:1Q6503 4.1 39.1 1.0
C3A B:HEM501 4.2 29.8 1.0
C2A B:HEM501 4.2 34.0 1.0
C2D B:HEM501 4.2 29.1 1.0
C3D B:HEM501 4.2 27.6 1.0
CA B:CYS186 4.2 30.1 1.0
C3C B:HEM501 4.2 30.6 1.0
C2C B:HEM501 4.2 31.7 1.0
C2B B:HEM501 4.2 28.5 1.0
C3B B:HEM501 4.3 28.1 1.0
NE1 B:TRP180 4.3 28.7 1.0
C22 B:1Q6503 4.5 33.6 1.0
C25 B:1Q6503 4.7 38.4 1.0
N B:GLY188 4.9 26.9 1.0
CD1 B:TRP180 5.0 29.5 1.0

Reference:

Q.Jing, H.Li, G.Chreifi, L.J.Roman, P.Martasek, T.L.Poulos, R.B.Silverman. Chiral Linkers to Improve Selectivity of Double-Headed Neuronal Nitric Oxide Synthase Inhibitors. Bioorg.Med.Chem.Lett. V. 23 5674 2013.
ISSN: ISSN 0960-894X
PubMed: 23993333
DOI: 10.1016/J.BMCL.2013.08.034
Page generated: Sun Dec 13 15:39:13 2020

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