Iron in PDB 3e68: Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C130232

All present enzymatic activity of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C130232:
1.14.13.39;

The structure of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C130232, PDB code: 3e68 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.Stueh, 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)	19.63 / 2.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.779, 213.779, 115.750, 90.00, 90.00, 120.00
R / Rfree (%)	24.7 / 27.5

The binding sites of Iron atom in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C130232 (pdb code 3e68). 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-C130232, PDB code: 3e68:
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-C130232


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-C130232 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:30.3 occ:1.00 FE A:HEM901 0.0 30.3 1.0 NA A:HEM901 2.0 27.1 1.0 NB A:HEM901 2.1 27.1 1.0 ND A:HEM901 2.1 30.6 1.0 NC A:HEM901 2.1 31.1 1.0 SG A:CYS194 2.6 32.7 1.0 C1B A:HEM901 3.1 26.7 1.0 C4A A:HEM901 3.1 27.7 1.0 C1D A:HEM901 3.1 30.2 1.0 C4D A:HEM901 3.1 30.6 1.0 C1A A:HEM901 3.1 29.0 1.0 C4B A:HEM901 3.1 27.9 1.0 C4C A:HEM901 3.1 30.7 1.0 C1C A:HEM901 3.2 30.4 1.0 CB A:CYS194 3.4 31.9 1.0 CHB A:HEM901 3.4 27.1 1.0 CHD A:HEM901 3.5 30.4 1.0 CHA A:HEM901 3.5 29.9 1.0 CHC A:HEM901 3.5 29.2 1.0 CA A:CYS194 4.0 32.8 1.0 C1 A:AT6905 4.1 26.2 1.0 C2 A:AT6905 4.1 26.4 1.0 C9 A:AT6905 4.1 25.4 1.0 C2B A:HEM901 4.3 26.2 1.0 C3A A:HEM901 4.3 26.5 1.0 C2D A:HEM901 4.3 28.7 1.0 C3D A:HEM901 4.3 29.5 1.0 C2A A:HEM901 4.4 26.9 1.0 C3B A:HEM901 4.4 26.3 1.0 C2C A:HEM901 4.4 30.3 1.0 C3C A:HEM901 4.4 31.3 1.0 NE1 A:TRP188 4.5 33.9 1.0 N A:GLY196 4.7 32.4 1.0 C A:CYS194 4.7 33.9 1.0 C3 A:AT6905 4.7 26.2 1.0 N A:ILE195 4.7 33.9 1.0 C6 A:AT6905 4.7 27.1 1.0

Iron binding site 2 out of 2 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar-C130232


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-C130232 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1901 b:28.9 occ:1.00 FE B:HEM1901 0.0 28.9 1.0 NA B:HEM1901 2.0 24.1 1.0 ND B:HEM1901 2.1 28.9 1.0 NB B:HEM1901 2.1 25.7 1.0 NC B:HEM1901 2.1 29.3 1.0 SG B:CYS194 2.5 31.6 1.0 C4A B:HEM1901 3.1 24.0 1.0 C1A B:HEM1901 3.1 26.0 1.0 C4D B:HEM1901 3.1 30.3 1.0 C1D B:HEM1901 3.1 29.9 1.0 C1B B:HEM1901 3.1 25.5 1.0 C1C B:HEM1901 3.1 29.9 1.0 C4B B:HEM1901 3.1 25.2 1.0 C4C B:HEM1901 3.1 29.5 1.0 CB B:CYS194 3.4 28.3 1.0 CHC B:HEM1901 3.4 27.7 1.0 CHA B:HEM1901 3.4 27.7 1.0 CHB B:HEM1901 3.4 24.9 1.0 CHD B:HEM1901 3.5 30.7 1.0 C1 B:AT61905 4.0 26.9 1.0 C2 B:AT61905 4.0 28.2 1.0 C9 B:AT61905 4.1 28.1 1.0 CA B:CYS194 4.1 30.1 1.0 C3A B:HEM1901 4.3 22.3 1.0 C2A B:HEM1901 4.3 23.0 1.0 C3D B:HEM1901 4.3 30.4 1.0 C2B B:HEM1901 4.3 23.9 1.0 C2D B:HEM1901 4.4 30.1 1.0 C3B B:HEM1901 4.4 24.1 1.0 C2C B:HEM1901 4.4 29.7 1.0 C3C B:HEM1901 4.4 29.9 1.0 NE1 B:TRP188 4.5 31.8 1.0 C6 B:AT61905 4.7 27.7 1.0 C3 B:AT61905 4.7 28.6 1.0 C B:CYS194 4.8 30.8 1.0 N B:ILE195 4.9 30.1 1.0 N B:GLY196 4.9 29.7 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