Iron in PDB 3e65: Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011

All present enzymatic activity of Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011:
1.14.13.39;

The structure of Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011, PDB code: 3e65 was solved by R.J.Rosenfeld, E.D.Garcin, E.D.Getzoff, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 2.05
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.935, 213.935, 117.025, 90.00, 90.00, 120.00
R / Rfree (%)	24.9 / 27.1

The structure of Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011 also contains other interesting chemical elements:

Fluorine

(F)

2 atoms

The binding sites of Iron atom in the Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011 (pdb code 3e65). 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 Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011, PDB code: 3e65:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:31.2 occ:1.00 FE A:HEM901 0.0 31.2 1.0 NB A:HEM901 2.0 30.9 1.0 NC A:HEM901 2.0 29.5 1.0 ND A:HEM901 2.1 29.4 1.0 NA A:HEM901 2.1 30.7 1.0 SG A:CYS194 2.3 32.7 1.0 C1D A:HEM901 3.1 28.6 1.0 C4C A:HEM901 3.1 29.9 1.0 C1B A:HEM901 3.1 30.5 1.0 C4B A:HEM901 3.1 32.1 1.0 C1C A:HEM901 3.1 31.8 1.0 C4A A:HEM901 3.1 31.1 1.0 C4D A:HEM901 3.1 30.5 1.0 C1A A:HEM901 3.1 30.5 1.0 CB A:CYS194 3.2 28.7 1.0 C4 A:XXZ906 3.4 29.6 1.0 C3 A:XXZ906 3.4 30.0 1.0 CHD A:HEM901 3.4 28.6 1.0 CHC A:HEM901 3.4 31.0 1.0 CHB A:HEM901 3.5 29.6 1.0 CHA A:HEM901 3.5 31.7 1.0 C1 A:XXZ906 4.0 29.0 1.0 C2 A:XXZ906 4.1 28.9 1.0 CA A:CYS194 4.1 31.2 1.0 NE1 A:TRP188 4.2 28.3 1.0 C2D A:HEM901 4.3 28.5 1.0 C2B A:HEM901 4.3 32.2 1.0 C3D A:HEM901 4.3 28.3 1.0 C3B A:HEM901 4.3 31.7 1.0 C3C A:HEM901 4.3 30.2 1.0 C2C A:HEM901 4.3 31.8 1.0 C3A A:HEM901 4.3 31.0 1.0 C2A A:HEM901 4.3 29.9 1.0 C6 A:XXZ906 4.6 28.8 1.0 C7 A:XXZ906 4.7 29.9 1.0 F1 A:XXZ906 4.7 31.7 1.0 C A:CYS194 4.9 30.5 1.0 CD1 A:TRP188 4.9 28.7 1.0 N A:GLY196 4.9 33.0 1.0 N A:ILE195 5.0 32.8 1.0

Iron binding site 2 out of 2 in the Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:29.4 occ:1.00 FE B:HEM901 0.0 29.4 1.0 NC B:HEM901 2.0 27.2 1.0 ND B:HEM901 2.0 25.6 1.0 NB B:HEM901 2.0 30.6 1.0 NA B:HEM901 2.0 27.8 1.0 SG B:CYS194 2.4 32.8 1.0 C1C B:HEM901 3.1 30.1 1.0 C4D B:HEM901 3.1 27.0 1.0 C4A B:HEM901 3.1 30.1 1.0 C4B B:HEM901 3.1 29.4 1.0 C4C B:HEM901 3.1 28.5 1.0 C1B B:HEM901 3.1 30.4 1.0 C1D B:HEM901 3.1 26.9 1.0 C1A B:HEM901 3.1 28.9 1.0 CB B:CYS194 3.3 27.4 1.0 C3 B:XXZ907 3.4 32.0 1.0 C4 B:XXZ907 3.4 31.1 1.0 CHC B:HEM901 3.4 30.5 1.0 CHB B:HEM901 3.5 30.6 1.0 CHA B:HEM901 3.5 27.7 1.0 CHD B:HEM901 3.5 27.8 1.0 C2 B:XXZ907 4.0 29.9 1.0 C1 B:XXZ907 4.0 31.6 1.0 CA B:CYS194 4.2 29.2 1.0 NE1 B:TRP188 4.3 27.8 1.0 C3B B:HEM901 4.3 31.3 1.0 C2B B:HEM901 4.3 31.3 1.0 C3A B:HEM901 4.3 29.3 1.0 C2C B:HEM901 4.3 29.4 1.0 C3D B:HEM901 4.3 26.0 1.0 C3C B:HEM901 4.3 28.5 1.0 C2D B:HEM901 4.3 26.5 1.0 C2A B:HEM901 4.3 28.8 1.0 C6 B:XXZ907 4.6 29.1 1.0 C7 B:XXZ907 4.6 30.8 1.0 F1 B:XXZ907 4.6 34.8 1.0 CD1 B:TRP188 4.9 27.0 1.0 C B:CYS194 4.9 29.2 1.0 N B:GLY196 4.9 30.6 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