Iron in PDB 1jwj: Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with W457F Mutation at Tetrahydrobiopterin Binding Site

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with W457F Mutation at Tetrahydrobiopterin Binding Site:
1.14.13.39;

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with W457F Mutation at Tetrahydrobiopterin Binding Site, PDB code: 1jwj was solved by M.Aoyagi, A.S.Arvai, S.Ghosh, D.J.Stuehr, J.A.Tainer, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.41 / 2.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.603, 213.603, 116.892, 90.00, 90.00, 120.00
R / Rfree (%)	21.8 / 25.7

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with W457F Mutation at Tetrahydrobiopterin Binding Site (pdb code 1jwj). 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 W457F Mutation at Tetrahydrobiopterin Binding Site, PDB code: 1jwj:
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 W457F Mutation at Tetrahydrobiopterin Binding Site


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 W457F Mutation at Tetrahydrobiopterin Binding Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:27.1 occ:1.00 FE A:HEM801 0.0 27.1 1.0 NA A:HEM801 2.0 25.5 1.0 ND A:HEM801 2.0 27.8 1.0 NC A:HEM801 2.0 25.7 1.0 NB A:HEM801 2.1 25.2 1.0 SG A:CYS194 2.7 29.9 1.0 C1A A:HEM801 3.0 28.3 1.0 C4D A:HEM801 3.0 29.4 1.0 C4C A:HEM801 3.1 26.4 1.0 C1C A:HEM801 3.1 25.7 1.0 C4A A:HEM801 3.1 25.6 1.0 C1D A:HEM801 3.1 26.3 1.0 C1B A:HEM801 3.1 24.7 1.0 C4B A:HEM801 3.1 26.0 1.0 CHA A:HEM801 3.4 28.3 1.0 CB A:CYS194 3.4 30.9 1.0 CHD A:HEM801 3.4 26.2 1.0 CHC A:HEM801 3.4 24.1 1.0 CHB A:HEM801 3.5 23.8 1.0 CA A:CYS194 4.1 30.5 1.0 C3D A:HEM801 4.3 28.2 1.0 C3A A:HEM801 4.3 26.8 1.0 C2A A:HEM801 4.3 27.5 1.0 C2D A:HEM801 4.3 26.4 1.0 C2C A:HEM801 4.3 25.0 1.0 C3C A:HEM801 4.3 25.6 1.0 C2B A:HEM801 4.4 25.0 1.0 C3B A:HEM801 4.4 24.6 1.0 NE1 A:TRP188 4.5 29.1 1.0 N A:GLY196 4.8 33.1 1.0 N A:ILE195 4.8 32.6 1.0 C A:CYS194 4.8 31.9 1.0

Iron binding site 2 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Dimer (Delta 65) with W457F Mutation at Tetrahydrobiopterin Binding Site


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 W457F Mutation at Tetrahydrobiopterin Binding Site within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:27.6 occ:1.00 FE B:HEM901 0.0 27.6 1.0 NA B:HEM901 2.0 23.7 1.0 NB B:HEM901 2.0 23.1 1.0 NC B:HEM901 2.0 24.8 1.0 ND B:HEM901 2.0 24.5 1.0 SG B:CYS194 2.7 31.9 1.0 C1B B:HEM901 3.0 23.4 1.0 C4A B:HEM901 3.0 23.1 1.0 C1C B:HEM901 3.0 24.4 1.0 C1A B:HEM901 3.1 25.8 1.0 C4C B:HEM901 3.1 25.2 1.0 C4B B:HEM901 3.1 23.6 1.0 C4D B:HEM901 3.1 26.1 1.0 C1D B:HEM901 3.1 24.6 1.0 CB B:CYS194 3.4 33.5 1.0 CHC B:HEM901 3.4 24.3 1.0 CHB B:HEM901 3.4 20.8 1.0 CHD B:HEM901 3.4 24.1 1.0 CHA B:HEM901 3.4 26.5 1.0 CA B:CYS194 4.1 34.1 1.0 C2A B:HEM901 4.3 26.4 1.0 C2B B:HEM901 4.3 23.5 1.0 C3A B:HEM901 4.3 25.1 1.0 C2C B:HEM901 4.3 23.3 1.0 C3C B:HEM901 4.3 24.6 1.0 C3D B:HEM901 4.3 25.7 1.0 C3B B:HEM901 4.3 23.8 1.0 C2D B:HEM901 4.3 24.4 1.0 NE1 B:TRP188 4.3 23.9 1.0 N B:GLY196 4.8 30.9 1.0 N B:ILE195 4.8 32.1 1.0 C B:CYS194 4.8 34.5 1.0 CD1 B:TRP188 5.0 25.8 1.0

M.Aoyagi, A.S.Arvai, S.Ghosh, D.J.Stuehr, J.A.Tainer, E.D.Getzoff. Structures of Tetrahydrobiopterin Binding-Site Mutants of Inducible Nitric Oxide Synthase Oxygenase Dimer and Implicated Roles of TRP457. Biochemistry V. 40 12826 2001.
ISSN: ISSN 0006-2960
PubMed: 11669619
DOI: 10.1021/BI011183K