Iron in PDB 3nod: Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Product Analogue L-Thiocitrulline

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

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Product Analogue L-Thiocitrulline, PDB code: 3nod 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 / 2.70
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 (%)	22.7 / 28.6

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Product Analogue L-Thiocitrulline (pdb code 3nod). 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 Product Analogue L-Thiocitrulline, PDB code: 3nod:
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 Product Analogue L-Thiocitrulline


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 Product Analogue L-Thiocitrulline within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:32.2 occ:1.00 FE A:HEM901 0.0 32.2 1.0 NC A:HEM901 2.0 28.1 1.0 ND A:HEM901 2.0 35.4 1.0 NB A:HEM901 2.0 25.6 1.0 NA A:HEM901 2.1 28.4 1.0 SG A:CYS194 2.3 40.7 1.0 CB A:CYS194 3.0 37.7 1.0 C1B A:HEM901 3.0 30.7 1.0 C1C A:HEM901 3.0 30.5 1.0 C4B A:HEM901 3.1 32.9 1.0 C4C A:HEM901 3.1 36.9 1.0 C1D A:HEM901 3.1 37.6 1.0 C4D A:HEM901 3.1 36.7 1.0 C4A A:HEM901 3.1 26.5 1.0 C1A A:HEM901 3.1 30.8 1.0 CHC A:HEM901 3.4 28.5 1.0 CHD A:HEM901 3.4 37.0 1.0 CHB A:HEM901 3.4 29.5 1.0 CHA A:HEM901 3.4 38.3 1.0 CA A:CYS194 3.9 41.2 1.0 NE1 A:TRP188 4.2 52.7 1.0 S A:SCI906 4.2 75.5 1.0 C2B A:HEM901 4.3 36.7 1.0 C3D A:HEM901 4.3 26.6 1.0 C2C A:HEM901 4.3 35.5 1.0 C3B A:HEM901 4.3 40.5 1.0 C3A A:HEM901 4.3 24.1 1.0 C2D A:HEM901 4.3 27.3 1.0 C2A A:HEM901 4.3 24.8 1.0 C3C A:HEM901 4.3 37.9 1.0 C A:CYS194 4.6 42.4 1.0 N A:GLY196 4.7 37.0 1.0 N A:ILE195 4.7 42.6 1.0 CD1 A:TRP188 4.9 54.4 1.0 CZ A:SCI906 4.9 68.2 1.0

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


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 Product Analogue L-Thiocitrulline within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:32.7 occ:1.00 FE B:HEM901 0.0 32.7 1.0 ND B:HEM901 2.0 33.6 1.0 NC B:HEM901 2.0 34.6 1.0 NB B:HEM901 2.0 32.9 1.0 NA B:HEM901 2.0 28.7 1.0 SG B:CYS194 2.3 36.9 1.0 C1C B:HEM901 3.0 35.5 1.0 C1B B:HEM901 3.0 36.2 1.0 C4A B:HEM901 3.0 31.5 1.0 C4D B:HEM901 3.0 35.2 1.0 C1D B:HEM901 3.0 37.1 1.0 C4B B:HEM901 3.1 33.4 1.0 C4C B:HEM901 3.1 40.0 1.0 C1A B:HEM901 3.1 27.0 1.0 CB B:CYS194 3.2 34.3 1.0 CHC B:HEM901 3.4 34.2 1.0 CHB B:HEM901 3.4 36.0 1.0 CHD B:HEM901 3.4 38.7 1.0 CHA B:HEM901 3.4 32.3 1.0 S B:SCI906 4.0 66.7 1.0 CA B:CYS194 4.0 35.5 1.0 C3D B:HEM901 4.2 33.7 1.0 C3A B:HEM901 4.3 23.6 1.0 C2A B:HEM901 4.3 23.6 1.0 C2B B:HEM901 4.3 35.9 1.0 C3B B:HEM901 4.3 35.7 1.0 NE1 B:TRP188 4.3 38.2 1.0 C2C B:HEM901 4.3 35.7 1.0 C2D B:HEM901 4.3 31.8 1.0 C3C B:HEM901 4.3 36.8 1.0 N B:ILE195 4.8 35.4 1.0 C B:CYS194 4.8 35.2 1.0 CZ B:SCI906 4.8 67.5 1.0 N B:GLY196 4.9 39.9 1.0 CD1 B:TRP188 4.9 42.6 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