Iron in PDB 3e7i: Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864

All present enzymatic activity of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864:
1.14.13.39;

The structure of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864, PDB code: 3e7i was solved by E.D.Garcin, A.S.Arvai, R.J.Rosenfeld, M.D.Kroeger, B.R.Crane, G.Andersson, G.Andrews, P.J.Hamley, P.R.Mallinder, D.J.Nicholls, S.A.St-Gallay, A.C.Tinker, N.P.Gensmantel, A.Mete, D.R.Cheshire, S.Connolly, D.J.Stuehr, A.Aberg, A.V.Wallace, 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)	19.99 / 2.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.967, 213.967, 113.130, 90.00, 90.00, 120.00
R / Rfree (%)	23.9 / 29.5

The structure of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864 also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Zinc	(Zn)	2 atoms

The binding sites of Iron atom in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864 (pdb code 3e7i). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864, PDB code: 3e7i:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:46.6 occ:1.00 FE A:HEM901 0.0 46.6 1.0 ND A:HEM901 2.0 44.7 1.0 NA A:HEM901 2.1 46.2 1.0 NC A:HEM901 2.1 41.8 1.0 NB A:HEM901 2.1 42.9 1.0 SG A:CYS194 2.5 51.4 1.0 C4D A:HEM901 3.0 46.3 1.0 C1D A:HEM901 3.1 44.5 1.0 C1A A:HEM901 3.1 47.6 1.0 C4C A:HEM901 3.1 41.8 1.0 C1B A:HEM901 3.1 44.4 1.0 C4A A:HEM901 3.1 46.8 1.0 C1C A:HEM901 3.1 40.9 1.0 C4B A:HEM901 3.2 42.9 1.0 CB A:CYS194 3.3 53.8 1.0 CHA A:HEM901 3.4 47.9 1.0 CHD A:HEM901 3.4 43.1 1.0 CHB A:HEM901 3.5 46.0 1.0 CHC A:HEM901 3.5 41.8 1.0 C3 A:B2906 3.6 52.8 1.0 C2 A:B2906 3.7 52.6 1.0 CA A:CYS194 4.0 54.3 1.0 C4 A:B2906 4.0 52.8 1.0 C1 A:B2906 4.1 52.8 1.0 C3D A:HEM901 4.2 47.3 1.0 C2D A:HEM901 4.3 45.8 1.0 C2B A:HEM901 4.3 44.2 1.0 C2A A:HEM901 4.4 49.1 1.0 C3A A:HEM901 4.4 48.4 1.0 C3C A:HEM901 4.4 39.8 1.0 C2C A:HEM901 4.4 38.3 1.0 C4A A:B2906 4.4 51.9 1.0 C3B A:HEM901 4.4 44.1 1.0 C8A A:B2906 4.5 51.5 1.0 NE1 A:TRP188 4.5 53.3 1.0 F15 A:B2906 4.6 55.7 1.0 N A:ILE195 4.7 57.0 1.0 C A:CYS194 4.8 56.6 1.0 N A:GLY196 4.9 57.5 1.0

Iron binding site 2 out of 2 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2901 b:47.7 occ:1.00 FE B:HEM2901 0.0 47.7 1.0 NC B:HEM2901 2.0 48.8 1.0 ND B:HEM2901 2.0 48.7 1.0 NA B:HEM2901 2.1 48.6 1.0 NB B:HEM2901 2.1 50.2 1.0 SG B:CYS194 2.9 49.6 1.0 C4C B:HEM2901 3.0 48.5 1.0 C1C B:HEM2901 3.1 47.7 1.0 C1D B:HEM2901 3.1 49.3 1.0 C4D B:HEM2901 3.1 48.5 1.0 C1A B:HEM2901 3.1 48.2 1.0 C4A B:HEM2901 3.1 48.4 1.0 C1B B:HEM2901 3.2 50.0 1.0 C4B B:HEM2901 3.2 49.8 1.0 CB B:CYS194 3.3 51.5 1.0 CHD B:HEM2901 3.4 48.8 1.0 CHA B:HEM2901 3.4 49.5 1.0 CHC B:HEM2901 3.5 49.2 1.0 C3 B:B22906 3.5 52.9 1.0 CHB B:HEM2901 3.5 48.3 1.0 C2 B:B22906 3.6 53.8 1.0 C4 B:B22906 3.8 53.2 1.0 CA B:CYS194 4.0 51.7 1.0 C1 B:B22906 4.0 53.7 1.0 C4A B:B22906 4.2 53.0 1.0 C3C B:HEM2901 4.3 49.1 1.0 C2C B:HEM2901 4.3 47.8 1.0 C8A B:B22906 4.3 54.2 1.0 C3D B:HEM2901 4.3 47.8 1.0 C2A B:HEM2901 4.3 48.9 1.0 C2D B:HEM2901 4.4 48.1 1.0 C2B B:HEM2901 4.4 50.2 1.0 C3A B:HEM2901 4.4 49.2 1.0 F15 B:B22906 4.4 57.4 1.0 C3B B:HEM2901 4.4 50.3 1.0 NE1 B:TRP188 4.5 55.5 1.0 C B:CYS194 4.8 51.9 1.0 N B:ILE195 4.9 53.0 1.0 CD1 B:TRP188 4.9 55.6 1.0

E.D.Garcin, A.S.Arvai, R.J.Rosenfeld, M.D.Kroeger, B.R.Crane, G.Andersson, G.Andrews, P.J.Hamley, P.R.Mallinder, D.J.Nicholls, S.A.St-Gallay, A.C.Tinker, N.P.Gensmantel, A.Mete, D.R.Cheshire, S.Connolly, D.J.Stuehr, A.Aberg, A.V.Wallace, J.A.Tainer, E.D.Getzoff. Anchored Plasticity Opens Doors For Selective Inhibitor Design in Nitric Oxide Synthase. Nat.Chem.Biol. V. 4 700 2008.
ISSN: ISSN 1552-4450
PubMed: 18849972
DOI: 10.1038/NCHEMBIO.115