Iron in PDB 3e7t: Structure of Murine Inos Oxygenase Domain with Inhibitor Ar- C102222

All present enzymatic activity of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar- C102222:
1.14.13.39;

The structure of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar- C102222, PDB code: 3e7t 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 / 2.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	214.156, 214.156, 116.950, 90.00, 90.00, 120.00
R / Rfree (%)	23.2 / 26.3

The structure of Structure of Murine Inos Oxygenase Domain with Inhibitor Ar- C102222 also contains other interesting chemical elements:

Fluorine

(F)

4 atoms

The binding sites of Iron atom in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar- C102222 (pdb code 3e7t). 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- C102222, PDB code: 3e7t:
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- C102222


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- C102222 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:30.2 occ:1.00 FE A:HEM901 0.0 30.2 1.0 NA A:HEM901 2.0 27.1 1.0 ND A:HEM901 2.1 28.8 1.0 NB A:HEM901 2.1 27.3 1.0 NC A:HEM901 2.1 26.8 1.0 SG A:CYS194 2.4 35.0 1.0 C4A A:HEM901 3.1 26.5 1.0 C1B A:HEM901 3.1 25.5 1.0 C1A A:HEM901 3.1 28.6 1.0 C4D A:HEM901 3.1 29.3 1.0 C1D A:HEM901 3.1 29.1 1.0 C4C A:HEM901 3.1 27.7 1.0 C1C A:HEM901 3.1 27.4 1.0 C4B A:HEM901 3.2 27.7 1.0 C2 A:B14906 3.3 28.7 1.0 C3 A:B14906 3.4 29.1 1.0 CHB A:HEM901 3.4 24.3 1.0 CB A:CYS194 3.4 33.8 1.0 CHA A:HEM901 3.4 29.0 1.0 CHD A:HEM901 3.4 28.6 1.0 CHC A:HEM901 3.5 27.3 1.0 C1 A:B14906 3.9 29.5 1.0 C4 A:B14906 4.0 29.1 1.0 CA A:CYS194 4.1 35.2 1.0 C3A A:HEM901 4.3 26.3 1.0 C2B A:HEM901 4.3 25.8 1.0 C2C A:HEM901 4.4 28.0 1.0 C3D A:HEM901 4.4 29.5 1.0 C2D A:HEM901 4.4 28.6 1.0 C3C A:HEM901 4.4 27.0 1.0 C2A A:HEM901 4.4 27.0 1.0 C3B A:HEM901 4.4 26.3 1.0 NE1 A:TRP188 4.4 35.6 1.0 C4A A:B14906 4.5 27.2 1.0 C8A A:B14906 4.5 27.0 1.0 F10 A:B14906 4.5 33.2 1.0 F9 A:B14906 4.7 32.0 1.0 C A:CYS194 4.9 35.4 1.0

Iron binding site 2 out of 2 in the Structure of Murine Inos Oxygenase Domain with Inhibitor Ar- C102222


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- C102222 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:32.5 occ:1.00 FE B:HEM901 0.0 32.5 1.0 NA B:HEM901 2.1 28.5 1.0 NC B:HEM901 2.1 30.6 1.0 ND B:HEM901 2.1 29.9 1.0 NB B:HEM901 2.1 29.1 1.0 SG B:CYS194 2.6 34.9 1.0 C4A B:HEM901 3.1 29.7 1.0 C4C B:HEM901 3.1 32.2 1.0 C1B B:HEM901 3.1 29.0 1.0 C1D B:HEM901 3.1 30.7 1.0 C4D B:HEM901 3.1 30.1 1.0 C1C B:HEM901 3.1 30.8 1.0 C1A B:HEM901 3.1 29.1 1.0 C4B B:HEM901 3.1 29.1 1.0 C3 B:B14906 3.3 31.0 1.0 C2 B:B14906 3.3 30.8 1.0 CHD B:HEM901 3.4 31.3 1.0 CHB B:HEM901 3.4 29.2 1.0 CB B:CYS194 3.4 36.0 1.0 CHC B:HEM901 3.5 30.0 1.0 CHA B:HEM901 3.5 29.5 1.0 C4 B:B14906 3.9 32.1 1.0 C1 B:B14906 4.0 32.9 1.0 CA B:CYS194 4.2 37.5 1.0 C3A B:HEM901 4.3 29.4 1.0 C3C B:HEM901 4.3 32.8 1.0 C2B B:HEM901 4.3 28.0 1.0 C3D B:HEM901 4.4 29.4 1.0 C2D B:HEM901 4.4 29.0 1.0 C2A B:HEM901 4.4 29.3 1.0 C2C B:HEM901 4.4 32.2 1.0 C3B B:HEM901 4.4 26.9 1.0 C4A B:B14906 4.4 32.5 1.0 F9 B:B14906 4.5 34.3 1.0 C8A B:B14906 4.5 32.9 1.0 NE1 B:TRP188 4.5 33.2 1.0 F10 B:B14906 4.6 36.1 1.0 C B:CYS194 5.0 37.2 1.0 N B:GLY196 5.0 37.7 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