Fluorine 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:

Iron	(Fe)	2 atoms
Zinc	(Zn)	2 atoms

The binding sites of Fluorine 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 Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864, PDB code: 3e7i:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F 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:F906 b:55.7 occ:1.00 F15 A:B2906 0.0 55.7 1.0 C4 A:B2906 1.3 52.8 1.0 C3 A:B2906 2.3 52.8 1.0 C4A A:B2906 2.4 51.9 1.0 N14 A:B2906 2.6 50.0 1.0 C5 A:B2906 2.9 52.4 1.0 N A:TRP366 3.1 45.4 1.0 O A:TRP366 3.1 41.0 1.0 CA A:GLY365 3.3 46.6 1.0 C1B A:HEM901 3.4 44.4 1.0 NB A:HEM901 3.5 42.9 1.0 CG A:PRO344 3.6 55.7 1.0 C A:GLY365 3.6 46.6 1.0 N A:GLY365 3.6 47.8 1.0 C2 A:B2906 3.6 52.6 1.0 C2B A:HEM901 3.7 44.2 1.0 C4B A:HEM901 3.7 42.9 1.0 C8A A:B2906 3.7 51.5 1.0 CHB A:HEM901 3.7 46.0 1.0 C A:TRP366 3.8 41.8 1.0 C3B A:HEM901 3.8 44.1 1.0 CA A:TRP366 4.0 43.1 1.0 C4A A:HEM901 4.1 46.8 1.0 C1 A:B2906 4.1 52.8 1.0 CB A:PRO344 4.2 54.4 1.0 N6 A:B2906 4.2 52.8 1.0 CHC A:HEM901 4.3 41.8 1.0 NA A:HEM901 4.4 46.2 1.0 CMB A:HEM901 4.4 45.1 1.0 O A:PRO344 4.5 58.2 1.0 FE A:HEM901 4.6 46.6 1.0 CAB A:HEM901 4.7 43.7 1.0 O A:GLY365 4.7 47.2 1.0 N A:TYR367 4.7 43.6 1.0 N8 A:B2906 4.8 52.5 1.0 C A:ASN364 4.8 49.1 1.0 C1C A:HEM901 4.9 40.9 1.0 CD A:PRO344 5.0 56.4 1.0 NC A:HEM901 5.0 41.8 1.0 C3A A:HEM901 5.0 48.4 1.0

Fluorine binding site 2 out of 3 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F 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 A:F907 b:0.1 occ:1.00 F15 A:B2907 0.0 0.1 1.0 C4 A:B2907 1.3 0.8 1.0 C3 A:B2907 2.4 0.6 1.0 C4A A:B2907 2.4 0.8 1.0 N14 A:B2907 2.7 0.9 1.0 C5 A:B2907 2.9 0.4 1.0 C2 A:B2907 3.6 0.0 1.0 C8A A:B2907 3.7 0.4 1.0 C1 A:B2907 4.2 0.7 1.0 N6 A:B2907 4.3 0.2 1.0 OE1 A:GLU387 4.6 77.4 1.0 OD1 A:ASN384 4.7 77.0 1.0 N8 A:B2907 4.8 0.1 1.0

Fluorine binding site 3 out of 3 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C94864 within 5.0Å range: probe atom residue distance (Å) B Occ B:F2906 b:57.4 occ:1.00 F15 B:B22906 0.0 57.4 1.0 C4 B:B22906 1.3 53.2 1.0 C3 B:B22906 2.3 52.9 1.0 C4A B:B22906 2.4 53.0 1.0 N14 B:B22906 2.7 52.9 1.0 C5 B:B22906 2.9 53.0 1.0 O B:TRP366 3.0 49.9 1.0 N B:TRP366 3.3 53.3 1.0 C B:GLY365 3.3 55.5 1.0 C1B B:HEM2901 3.3 50.0 1.0 NB B:HEM2901 3.3 50.2 1.0 CA B:GLY365 3.4 53.4 1.0 C4B B:HEM2901 3.5 49.8 1.0 C2B B:HEM2901 3.5 50.2 1.0 N B:GLY365 3.6 51.7 1.0 C2 B:B22906 3.6 53.8 1.0 C8A B:B22906 3.7 54.2 1.0 C3B B:HEM2901 3.7 50.3 1.0 CHB B:HEM2901 3.7 48.3 1.0 CG B:PRO344 3.7 49.4 1.0 C B:TRP366 3.7 49.9 1.0 O B:GLY365 3.9 58.0 1.0 CA B:TRP366 4.0 50.5 1.0 C1 B:B22906 4.1 53.7 1.0 C4A B:HEM2901 4.2 48.4 1.0 CHC B:HEM2901 4.2 49.2 1.0 N6 B:B22906 4.2 54.8 1.0 CB B:PRO344 4.3 49.9 1.0 NA B:HEM2901 4.4 48.6 1.0 CMB B:HEM2901 4.4 48.1 1.0 O B:PRO344 4.4 51.1 1.0 FE B:HEM2901 4.4 47.7 1.0 CAB B:HEM2901 4.6 51.2 1.0 C B:ASN364 4.7 51.7 1.0 C1C B:HEM2901 4.8 47.7 1.0 N8 B:B22906 4.8 56.0 1.0 N B:TYR367 4.8 49.9 1.0 NC B:HEM2901 4.9 48.8 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