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Iron in PDB 5fvu: Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine

Enzymatic activity of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine

All present enzymatic activity of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine:
1.14.13.39;

Protein crystallography data

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine, PDB code: 5fvu 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) 48.794 / 2.22
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.330, 121.670, 163.400, 90.00, 90.00, 90.00
R / Rfree (%) 17.68 / 24.84

Other elements in 5fvu:

The structure of Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine (pdb code 5fvu). 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 Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine, PDB code: 5fvu:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 5fvu

Go back to Iron Binding Sites List in 5fvu
Iron binding site 1 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-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 Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe750

b:26.1
occ:1.00
 FE A:HEM750 0.0 26.1 1.0
NB A:HEM750 2.0 31.5 1.0
NC A:HEM750 2.0 22.7 1.0
NA A:HEM750 2.0 29.1 1.0
ND A:HEM750 2.1 19.2 1.0
SG A:CYS420 2.3 29.8 1.0
C4B A:HEM750 3.0 30.1 1.0
C1B A:HEM750 3.0 38.8 1.0
C1C A:HEM750 3.0 26.9 1.0
C4C A:HEM750 3.1 21.9 1.0
C4A A:HEM750 3.1 28.2 1.0
C1A A:HEM750 3.1 25.7 1.0
C1D A:HEM750 3.1 23.7 1.0
C4D A:HEM750 3.2 26.8 1.0
CB A:CYS420 3.4 21.9 1.0
CHC A:HEM750 3.4 27.9 1.0
CHB A:HEM750 3.4 32.9 1.0
CHD A:HEM750 3.4 26.0 1.0
CHA A:HEM750 3.5 22.5 1.0
C03 A:W64800 4.0 27.1 1.0
CA A:CYS420 4.1 24.1 1.0
C04 A:W64800 4.2 27.5 1.0
C07 A:W64800 4.2 24.8 1.0
C2B A:HEM750 4.2 26.9 1.0
C3B A:HEM750 4.2 32.6 1.0
C2C A:HEM750 4.3 21.4 1.0
C3C A:HEM750 4.3 25.5 1.0
C3A A:HEM750 4.3 20.4 1.0
C2A A:HEM750 4.3 23.6 1.0
C2D A:HEM750 4.4 20.0 1.0
C3D A:HEM750 4.4 24.5 1.0
NE1 A:TRP414 4.4 28.3 1.0
N A:GLY422 4.7 19.4 1.0
C02 A:W64800 4.7 32.6 1.0
C A:CYS420 4.8 25.4 1.0
N A:VAL421 4.9 22.9 1.0
C05 A:W64800 4.9 33.2 1.0
CA A:GLY422 5.0 30.3 1.0

Iron binding site 2 out of 2 in 5fvu

Go back to Iron Binding Sites List in 5fvu
Iron binding site 2 out of 2 in the Structure of Human Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-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 Nnos R354A G357D Mutant Heme Domain in Complex with 4-Methyl-6-(2-(5-(4-Methylpiperazin-1-Yl) Pyridin-3-Yl)Ethyl)Pyridin-2-Amine within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe750

b:32.8
occ:1.00
 FE B:HEM750 0.0 32.8 1.0
NC B:HEM750 2.0 28.4 1.0
ND B:HEM750 2.1 25.7 1.0
NB B:HEM750 2.1 35.0 1.0
NA B:HEM750 2.1 32.5 1.0
SG B:CYS420 2.3 36.7 1.0
C1C B:HEM750 3.0 34.4 1.0
C4C B:HEM750 3.0 31.6 1.0
C4B B:HEM750 3.1 36.6 1.0
C1D B:HEM750 3.1 32.8 1.0
C4D B:HEM750 3.1 35.6 1.0
C1B B:HEM750 3.1 41.7 1.0
C1A B:HEM750 3.1 33.6 1.0
C4A B:HEM750 3.2 35.6 1.0
CB B:CYS420 3.3 22.7 1.0
CHD B:HEM750 3.4 32.3 1.0
CHC B:HEM750 3.4 38.8 1.0
CHA B:HEM750 3.5 30.4 1.0
CHB B:HEM750 3.5 40.3 1.0
C03 B:W64800 3.9 20.7 1.0
C07 B:W64800 3.9 34.6 1.0
C04 B:W64800 4.0 27.9 1.0
CA B:CYS420 4.2 22.8 1.0
C3C B:HEM750 4.3 31.6 1.0
C2C B:HEM750 4.3 35.2 1.0
C3B B:HEM750 4.3 37.9 1.0
C2B B:HEM750 4.3 35.3 1.0
C3D B:HEM750 4.3 35.4 1.0
C2D B:HEM750 4.3 30.2 1.0
C2A B:HEM750 4.4 29.6 1.0
C3A B:HEM750 4.4 30.2 1.0
NE1 B:TRP414 4.4 37.8 1.0
C02 B:W64800 4.6 24.9 1.0
C05 B:W64800 4.8 33.5 1.0
N B:GLY422 4.9 34.9 1.0
C B:CYS420 4.9 24.2 1.0
N B:VAL421 4.9 22.8 1.0

Reference:

H.Wang, Y.Qin, H.Li, L.J.Roman, P.Martasek, T.L.Poulos, R.B.Silverman. Potent and Selective Human Neuronal Nitric Oxide Synthase Inhibition By Optimization of the 2-Aminopyridine-Based Scaffold with A Pyridine Linker. J.Med.Chem. V. 59 4913 2016.
ISSN: ISSN 0022-2623
PubMed: 27050842
DOI: 10.1021/ACS.JMEDCHEM.6B00273
Page generated: Tue Aug 6 01:21:33 2024

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