Iron in PDB 2nod: Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Water Bound in Active Center

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Water Bound in Active Center:
1.14.13.39;

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Water Bound in Active Center, PDB code: 2nod 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 (%)	22.4 / 28.9

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Water Bound in Active Center (pdb code 2nod). 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 Water Bound in Active Center, PDB code: 2nod:
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 Water Bound in Active Center


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 Water Bound in Active Center within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:24.8 occ:1.00 FE A:HEM901 0.0 24.8 1.0 ND A:HEM901 2.0 30.3 1.0 NA A:HEM901 2.0 24.2 1.0 NC A:HEM901 2.0 27.3 1.0 NB A:HEM901 2.0 20.1 1.0 SG A:CYS194 2.3 36.0 1.0 C4D A:HEM901 3.0 30.9 1.0 C1B A:HEM901 3.0 22.2 1.0 C4A A:HEM901 3.0 24.0 1.0 C1D A:HEM901 3.0 33.0 1.0 C1A A:HEM901 3.0 28.8 1.0 CB A:CYS194 3.0 26.4 1.0 C1C A:HEM901 3.1 24.8 1.0 C4C A:HEM901 3.1 31.2 1.0 C4B A:HEM901 3.1 25.6 1.0 CHA A:HEM901 3.4 33.0 1.0 CHB A:HEM901 3.4 25.0 1.0 CHD A:HEM901 3.4 28.0 1.0 CHC A:HEM901 3.4 24.4 1.0 CA A:CYS194 3.9 30.0 1.0 C3D A:HEM901 4.2 22.8 1.0 C2B A:HEM901 4.2 29.3 1.0 C3A A:HEM901 4.3 20.7 1.0 C2A A:HEM901 4.3 22.8 1.0 C2D A:HEM901 4.3 24.8 1.0 O A:HOH1132 4.3 39.2 1.0 C2C A:HEM901 4.3 27.8 1.0 C3B A:HEM901 4.3 29.4 1.0 C3C A:HEM901 4.3 27.7 1.0 NE1 A:TRP188 4.4 41.4 1.0 C A:CYS194 4.7 32.6 1.0 N A:GLY196 4.7 28.6 1.0 N A:ILE195 4.7 32.8 1.0

Iron binding site 2 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with Tetrahydrobiopterin and Water Bound in Active Center


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 Water Bound in Active Center within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:28.9 occ:1.00 FE B:HEM901 0.0 28.9 1.0 ND B:HEM901 2.0 31.2 1.0 NC B:HEM901 2.0 32.2 1.0 NB B:HEM901 2.0 27.0 1.0 NA B:HEM901 2.0 21.6 1.0 SG B:CYS194 2.4 34.6 1.0 C1D B:HEM901 3.0 30.6 1.0 C1C B:HEM901 3.0 30.9 1.0 C4D B:HEM901 3.0 29.8 1.0 C1B B:HEM901 3.0 30.1 1.0 C4A B:HEM901 3.0 23.4 1.0 C4B B:HEM901 3.0 23.1 1.0 C4C B:HEM901 3.0 30.7 1.0 C1A B:HEM901 3.0 22.1 1.0 CB B:CYS194 3.3 28.2 1.0 CHC B:HEM901 3.4 24.8 1.0 CHD B:HEM901 3.4 29.6 1.0 CHA B:HEM901 3.4 22.5 1.0 CHB B:HEM901 3.4 27.4 1.0 CA B:CYS194 4.1 30.0 1.0 C3D B:HEM901 4.3 29.5 1.0 C3A B:HEM901 4.3 20.4 1.0 C2A B:HEM901 4.3 21.2 1.0 C2C B:HEM901 4.3 27.6 1.0 O B:HOH1190 4.3 22.6 1.0 C2D B:HEM901 4.3 26.8 1.0 C2B B:HEM901 4.3 25.3 1.0 NE1 B:TRP188 4.3 28.7 1.0 C3C B:HEM901 4.3 28.0 1.0 C3B B:HEM901 4.3 26.3 1.0 C B:CYS194 4.9 31.2 1.0 N B:ILE195 4.9 31.3 1.0 CD1 B:TRP188 4.9 34.9 1.0 N B:GLY196 5.0 35.4 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