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Iron in PDB 1dwx: Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin

Enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin:
1.14.13.39;

Protein crystallography data

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin, PDB code: 1dwx was solved by B.R.Crane, A.S.Arvai, E.D.Getzoff, D.J.Stuehr, J.A.Tainer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.00 / 2.60
Space group P 61 2 2
Cell size a, b, c (Å), α, β, γ (°) 212.980, 212.980, 114.200, 90.00, 90.00, 120.00
R / Rfree (%) 23.8 / 27.8

Iron Binding Sites:

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin (pdb code 1dwx). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin, PDB code: 1dwx:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in 1dwx

Go back to Iron Binding Sites List in 1dwx
Iron binding site 1 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe901

b:25.2
occ:1.00
FE A:HEM901 0.0 25.2 1.0
NA A:HEM901 2.0 17.9 1.0
NC A:HEM901 2.0 27.0 1.0
ND A:HEM901 2.0 27.0 1.0
NB A:HEM901 2.1 21.3 1.0
SG A:CYS194 2.4 40.8 1.0
C1A A:HEM901 3.1 25.8 1.0
C4A A:HEM901 3.1 21.3 1.0
C1B A:HEM901 3.1 26.1 1.0
C4C A:HEM901 3.1 32.7 1.0
C1C A:HEM901 3.1 34.7 1.0
C1D A:HEM901 3.1 31.7 1.0
C4D A:HEM901 3.1 26.9 1.0
C4B A:HEM901 3.1 31.2 1.0
CB A:CYS194 3.2 29.7 1.0
CHA A:HEM901 3.4 27.9 1.0
CHD A:HEM901 3.4 32.5 1.0
CHB A:HEM901 3.4 20.3 1.0
CHC A:HEM901 3.4 31.6 1.0
CA A:CYS194 3.9 32.6 1.0
OH1 A:HAR906 4.0 35.7 1.0
NH1 A:HAR906 4.0 38.4 1.0
C2A A:HEM901 4.3 24.6 1.0
NE1 A:TRP188 4.3 39.0 1.0
C2B A:HEM901 4.3 31.9 1.0
C3A A:HEM901 4.3 23.2 1.0
C3D A:HEM901 4.3 24.2 1.0
C3C A:HEM901 4.3 37.0 1.0
C2D A:HEM901 4.3 25.8 1.0
C3B A:HEM901 4.3 30.6 1.0
C2C A:HEM901 4.3 38.7 1.0
N A:ILE195 4.7 36.7 1.0
CZ A:HAR906 4.7 36.5 1.0
C A:CYS194 4.7 37.5 1.0
N A:GLY196 4.8 31.7 1.0
CD1 A:TRP188 4.9 41.3 1.0

Iron binding site 2 out of 2 in 1dwx

Go back to Iron Binding Sites List in 1dwx
Iron binding site 2 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer N-Hydroxyarginine and Tetrahydrobiopterin within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe901

b:24.5
occ:1.00
FE B:HEM901 0.0 24.5 1.0
NC B:HEM901 2.0 26.6 1.0
NA B:HEM901 2.0 15.8 1.0
NB B:HEM901 2.0 23.9 1.0
ND B:HEM901 2.0 20.0 1.0
SG B:CYS194 2.4 32.2 1.0
C1C B:HEM901 3.0 29.8 1.0
C1B B:HEM901 3.1 29.0 1.0
C1A B:HEM901 3.1 23.4 1.0
C4A B:HEM901 3.1 24.1 1.0
C4C B:HEM901 3.1 33.6 1.0
C1D B:HEM901 3.1 23.5 1.0
C4B B:HEM901 3.1 25.0 1.0
C4D B:HEM901 3.1 23.8 1.0
CB B:CYS194 3.3 20.9 1.0
CHC B:HEM901 3.4 28.8 1.0
CHB B:HEM901 3.4 28.8 1.0
CHA B:HEM901 3.4 27.5 1.0
CHD B:HEM901 3.4 23.5 1.0
OH1 B:HAR906 3.8 29.5 1.0
NH1 B:HAR906 3.9 32.7 1.0
CA B:CYS194 4.1 26.9 1.0
NE1 B:TRP188 4.3 33.0 1.0
C2A B:HEM901 4.3 17.3 1.0
C2B B:HEM901 4.3 27.2 1.0
C3A B:HEM901 4.3 20.9 1.0
C2C B:HEM901 4.3 28.8 1.0
C2D B:HEM901 4.3 19.4 1.0
C3B B:HEM901 4.3 27.9 1.0
C3C B:HEM901 4.3 34.4 1.0
C3D B:HEM901 4.3 25.8 1.0
CZ B:HAR906 4.6 29.9 1.0
NH2 B:HAR906 4.9 22.0 1.0
C B:CYS194 4.9 31.1 1.0
N B:ILE195 4.9 31.2 1.0
CD1 B:TRP188 4.9 37.0 1.0
N B:GLY196 5.0 29.8 1.0

Reference:

B.R.Crane, A.S.Arvai, S.Ghosh, E.D.Getzoff, D.J.Stuehr, J.A.Tainer. Structures of the N(Omega)-Hydroxy-L-Arginine Complex of Inducible Nitric Oxide Synthase Oxygenase Dimer with Active Andinactive Pterins Biochemistry V. 39 4608 2000.
ISSN: ISSN 0006-2960
PubMed: 10769116
DOI: 10.1021/BI992409A
Page generated: Sun Dec 13 14:11:32 2020

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