Iron in PDB 1nod: Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine:
1.14.13.39;

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine, PDB code: 1nod 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)	20.00 / 2.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.000, 213.000, 114.200, 90.00, 90.00, 120.00
R / Rfree (%)	22.9 / 28.8

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine (pdb code 1nod). 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 (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine, PDB code: 1nod:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine


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 (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:42.4 occ:1.00 FE A:HEM901 0.0 42.4 1.0 NA A:HEM901 2.0 43.4 1.0 NB A:HEM901 2.0 36.9 1.0 NC A:HEM901 2.0 41.5 1.0 ND A:HEM901 2.0 47.5 1.0 SG A:CYS194 2.3 46.0 1.0 C1B A:HEM901 3.0 39.4 1.0 C4A A:HEM901 3.0 41.9 1.0 C4B A:HEM901 3.0 42.1 1.0 C4C A:HEM901 3.0 45.4 1.0 C1C A:HEM901 3.0 40.8 1.0 C1D A:HEM901 3.0 47.0 1.0 CB A:CYS194 3.0 40.8 1.0 C1A A:HEM901 3.1 47.7 1.0 C4D A:HEM901 3.1 45.9 1.0 CHB A:HEM901 3.4 41.7 1.0 CHD A:HEM901 3.4 44.8 1.0 CHC A:HEM901 3.4 40.6 1.0 CHA A:HEM901 3.4 48.2 1.0 CA A:CYS194 3.9 46.3 1.0 NH1 A:ARG906 4.1 37.7 0.6 C2B A:HEM901 4.2 42.0 1.0 O A:HOH1136 4.2 27.3 0.5 C3A A:HEM901 4.2 37.4 1.0 NE1 A:TRP188 4.3 61.4 1.0 C2A A:HEM901 4.3 41.6 1.0 C3B A:HEM901 4.3 43.8 1.0 C3D A:HEM901 4.3 33.1 1.0 C2C A:HEM901 4.3 44.6 1.0 C2D A:HEM901 4.3 33.3 1.0 C3C A:HEM901 4.3 45.9 1.0 N A:ILE195 4.6 45.9 1.0 N A:GLY196 4.6 44.8 1.0 C A:CYS194 4.6 46.7 1.0 O A:HOH1151 4.7 48.5 0.6 CZ A:ARG906 4.8 43.0 0.6 CD1 A:TRP188 5.0 64.1 1.0

Iron binding site 2 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine


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 (Delta 65) with Tetrahydrobiopterin and Substrate L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:42.6 occ:1.00 FE B:HEM901 0.0 42.6 1.0 NC B:HEM901 2.0 50.1 1.0 NB B:HEM901 2.0 45.8 1.0 NA B:HEM901 2.0 41.1 1.0 ND B:HEM901 2.0 49.2 1.0 SG B:CYS194 2.3 42.2 1.0 C1C B:HEM901 3.0 46.0 1.0 C4B B:HEM901 3.0 45.0 1.0 C1B B:HEM901 3.0 49.4 1.0 C4A B:HEM901 3.0 41.1 1.0 C4C B:HEM901 3.0 50.0 1.0 C1D B:HEM901 3.0 48.6 1.0 C1A B:HEM901 3.0 42.8 1.0 C4D B:HEM901 3.1 50.4 1.0 CB B:CYS194 3.2 45.4 1.0 CHC B:HEM901 3.3 45.0 1.0 CHD B:HEM901 3.4 52.2 1.0 CHB B:HEM901 3.4 46.6 1.0 CHA B:HEM901 3.4 43.7 1.0 NH1 B:ARG906 3.9 34.4 0.6 CA B:CYS194 4.0 48.0 1.0 O B:HOH1192 4.2 34.1 0.5 C3A B:HEM901 4.2 37.7 1.0 C2C B:HEM901 4.2 42.6 1.0 C3B B:HEM901 4.2 45.1 1.0 NE1 B:TRP188 4.2 47.1 1.0 C2A B:HEM901 4.2 36.1 1.0 C2B B:HEM901 4.3 45.8 1.0 C3D B:HEM901 4.3 46.4 1.0 C3C B:HEM901 4.3 43.4 1.0 C2D B:HEM901 4.3 46.5 1.0 CZ B:ARG906 4.7 39.4 0.6 N B:ILE195 4.8 44.4 1.0 C B:CYS194 4.8 47.7 1.0 O B:HOH1213 4.8 46.5 0.6 N B:GLY196 4.8 46.1 1.0 CD1 B:TRP188 4.9 52.3 1.0

B.R.Crane, A.S.Arvai, D.K.Ghosh, C.Wu, E.D.Getzoff, D.J.Stuehr, J.A.Tainer. Structure of Nitric Oxide Synthase Oxygenase Dimer with Pterin and Substrate. Science V. 279 2121 1998.
ISSN: ISSN 0036-8075
PubMed: 9516116
DOI: 10.1126/SCIENCE.279.5359.2121