Fluorine 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:

Iron

(Fe)

2 atoms

The binding sites of Fluorine 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 Fluorine atom.
In total 2 binding sites of Fluorine where determined in the Murine Inos Dimer with Heme, Pterin and Inhibitor Ar-C120011, PDB code: 3e65:
Jump to Fluorine binding site number: 1; 2;

Fluorine 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 Fluorine with other atoms in the F 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:F906 b:31.7 occ:1.00 F1 A:XXZ906 0.0 31.7 1.0 C2 A:XXZ906 1.3 28.9 1.0 C7 A:XXZ906 2.3 29.9 1.0 C3 A:XXZ906 2.4 30.0 1.0 N21 A:XXZ906 2.9 30.1 1.0 CG A:XXZ906 2.9 27.6 1.0 N A:GLY365 3.2 31.7 1.0 CA A:GLY365 3.2 32.7 1.0 O A:TRP366 3.2 31.5 1.0 N A:TRP366 3.3 32.7 1.0 C A:GLY365 3.3 34.0 1.0 NB A:HEM901 3.6 30.9 1.0 C1B A:HEM901 3.6 30.5 1.0 C6 A:XXZ906 3.6 28.8 1.0 C4 A:XXZ906 3.6 29.6 1.0 CG A:PRO344 3.6 33.0 1.0 C4B A:HEM901 3.7 32.1 1.0 O A:PRO344 3.8 33.7 1.0 C2B A:HEM901 3.8 32.2 1.0 C3B A:HEM901 3.9 31.7 1.0 C A:TRP366 3.9 31.0 1.0 CHB A:HEM901 4.0 29.6 1.0 CB A:PRO344 4.1 33.6 1.0 O A:GLY365 4.1 33.1 1.0 C1 A:XXZ906 4.1 29.0 1.0 CA A:TRP366 4.1 31.3 1.0 CHC A:HEM901 4.2 31.0 1.0 N20 A:XXZ906 4.3 27.6 1.0 C A:ASN364 4.3 31.0 1.0 C4A A:HEM901 4.4 31.1 1.0 NA A:HEM901 4.6 30.7 1.0 CAB A:HEM901 4.6 33.8 1.0 CMB A:HEM901 4.6 33.6 1.0 C A:PRO344 4.7 33.0 1.0 FE A:HEM901 4.7 31.2 1.0 C1C A:HEM901 4.8 31.8 1.0 CA A:ASN364 4.9 30.9 1.0 N1 A:XXZ906 4.9 29.6 1.0 N A:TYR367 4.9 30.7 1.0 CD A:PRO344 5.0 30.1 1.0 NC A:HEM901 5.0 29.5 1.0 CA A:PRO344 5.0 32.2 1.0

Fluorine 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 Fluorine with other atoms in the F 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:F907 b:34.8 occ:1.00 F1 B:XXZ907 0.0 34.8 1.0 C2 B:XXZ907 1.3 29.9 1.0 C3 B:XXZ907 2.3 32.0 1.0 C7 B:XXZ907 2.4 30.8 1.0 N21 B:XXZ907 2.9 30.7 1.0 CG B:XXZ907 3.0 28.8 1.0 O B:TRP366 3.1 30.4 1.0 CA B:GLY365 3.2 30.9 1.0 N B:TRP366 3.2 31.3 1.0 N B:GLY365 3.2 29.4 1.0 C B:GLY365 3.2 32.4 1.0 NB B:HEM901 3.4 30.6 1.0 C1B B:HEM901 3.4 30.4 1.0 C4B B:HEM901 3.6 29.4 1.0 C4 B:XXZ907 3.6 31.1 1.0 C6 B:XXZ907 3.6 29.1 1.0 C2B B:HEM901 3.7 31.3 1.0 CG B:PRO344 3.7 32.5 1.0 C3B B:HEM901 3.8 31.3 1.0 C B:TRP366 3.8 31.1 1.0 O B:PRO344 3.8 32.1 1.0 CHB B:HEM901 3.9 30.6 1.0 O B:GLY365 4.0 32.4 1.0 CA B:TRP366 4.0 30.4 1.0 C1 B:XXZ907 4.1 31.6 1.0 CB B:PRO344 4.1 32.7 1.0 CHC B:HEM901 4.2 30.5 1.0 N20 B:XXZ907 4.3 28.6 1.0 C4A B:HEM901 4.3 30.1 1.0 C B:ASN364 4.3 27.8 1.0 CAB B:HEM901 4.5 33.8 1.0 NA B:HEM901 4.5 27.8 1.0 CMB B:HEM901 4.5 31.6 1.0 FE B:HEM901 4.6 29.4 1.0 C B:PRO344 4.8 30.6 1.0 C1C B:HEM901 4.8 30.1 1.0 N1 B:XXZ907 4.9 28.9 1.0 N B:TYR367 4.9 29.8 1.0 CA B:ASN364 4.9 27.9 1.0 NC B:HEM901 5.0 27.2 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