Iron in PDB 1dwx: 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;

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

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 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 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

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