Iron in PDB 3eai: Structure of Inhibited Murine Inos Oxygenase Domain

All present enzymatic activity of Structure of Inhibited Murine Inos Oxygenase Domain:
1.14.13.39;

The structure of Structure of Inhibited Murine Inos Oxygenase Domain, PDB code: 3eai 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)	19.95 / 2.20
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.111, 213.111, 116.562, 90.00, 90.00, 120.00
R / Rfree (%)	22.3 / n/a

The binding sites of Iron atom in the Structure of Inhibited Murine Inos Oxygenase Domain (pdb code 3eai). 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 Inhibited Murine Inos Oxygenase Domain, PDB code: 3eai:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Inhibited Murine Inos Oxygenase Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Inhibited Murine Inos Oxygenase Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:33.8 occ:1.00 FE A:HEM901 0.0 33.8 1.0 NA A:HEM901 2.0 28.2 1.0 NB A:HEM901 2.0 28.7 1.0 ND A:HEM901 2.0 29.1 1.0 NC A:HEM901 2.0 28.8 1.0 SG A:CYS194 2.6 36.5 1.0 C1B A:HEM901 3.0 27.9 1.0 C4A A:HEM901 3.0 28.5 1.0 C4D A:HEM901 3.1 30.7 1.0 C1A A:HEM901 3.1 30.6 1.0 C1C A:HEM901 3.1 29.8 1.0 C4C A:HEM901 3.1 29.9 1.0 C1D A:HEM901 3.1 28.0 1.0 C4B A:HEM901 3.1 28.2 1.0 CHB A:HEM901 3.4 28.3 1.0 CHA A:HEM901 3.4 29.8 1.0 CHC A:HEM901 3.4 29.0 1.0 CB A:CYS194 3.4 32.9 1.0 CHD A:HEM901 3.4 30.4 1.0 O18 A:328905 3.8 28.3 1.0 C19 A:328905 3.9 28.7 1.0 CA A:CYS194 4.1 34.7 1.0 C9 A:328905 4.2 31.2 1.0 C20 A:328905 4.3 28.1 1.0 C3D A:HEM901 4.3 30.2 1.0 C3A A:HEM901 4.3 27.6 1.0 C2B A:HEM901 4.3 26.4 1.0 C2D A:HEM901 4.3 28.1 1.0 C2A A:HEM901 4.3 28.3 1.0 C2C A:HEM901 4.3 29.2 1.0 C3C A:HEM901 4.3 28.1 1.0 C3B A:HEM901 4.3 26.3 1.0 C24 A:328905 4.5 27.9 1.0 NE1 A:TRP188 4.5 30.6 1.0 C A:CYS194 4.8 35.0 1.0 N A:ILE195 4.8 35.5 1.0 N A:GLY196 4.8 33.6 1.0

Iron binding site 2 out of 2 in the Structure of Inhibited Murine Inos Oxygenase Domain


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Inhibited Murine Inos Oxygenase Domain within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe2901 b:29.3 occ:1.00 FE B:HEM2901 0.0 29.3 1.0 NA B:HEM2901 2.0 22.0 1.0 NB B:HEM2901 2.0 23.1 1.0 NC B:HEM2901 2.0 25.4 1.0 ND B:HEM2901 2.0 25.0 1.0 SG B:CYS194 2.5 30.2 1.0 C4A B:HEM2901 3.0 23.9 1.0 C1B B:HEM2901 3.0 22.0 1.0 C1A B:HEM2901 3.1 24.2 1.0 C1C B:HEM2901 3.1 27.6 1.0 C4B B:HEM2901 3.1 22.9 1.0 C1D B:HEM2901 3.1 25.5 1.0 C4D B:HEM2901 3.1 27.0 1.0 C4C B:HEM2901 3.1 25.2 1.0 CHB B:HEM2901 3.4 22.1 1.0 CB B:CYS194 3.4 28.7 1.0 CHC B:HEM2901 3.4 24.9 1.0 CHD B:HEM2901 3.4 25.2 1.0 CHA B:HEM2901 3.4 26.0 1.0 O18 B:3282905 3.7 27.1 1.0 C19 B:3282905 4.0 23.8 1.0 CA B:CYS194 4.1 32.2 1.0 C9 B:3282905 4.1 27.9 1.0 C3A B:HEM2901 4.3 22.2 1.0 C2A B:HEM2901 4.3 22.7 1.0 C2B B:HEM2901 4.3 19.7 1.0 C3D B:HEM2901 4.3 27.7 1.0 C2D B:HEM2901 4.3 25.6 1.0 C20 B:3282905 4.3 21.5 1.0 C3B B:HEM2901 4.3 20.5 1.0 C2C B:HEM2901 4.3 27.7 1.0 C3C B:HEM2901 4.3 25.7 1.0 NE1 B:TRP188 4.4 26.8 1.0 C24 B:3282905 4.5 24.0 1.0 N B:GLY196 4.8 30.9 1.0 N B:ILE195 4.8 33.1 1.0 C B:CYS194 4.9 32.9 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