Iron in PDB 3e67: Murine Inos Dimer with Inhibitor 4-Map Bound

All present enzymatic activity of Murine Inos Dimer with Inhibitor 4-Map Bound:
1.14.13.39;

The structure of Murine Inos Dimer with Inhibitor 4-Map Bound, PDB code: 3e67 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)	19.99 / 2.60
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	214.093, 214.093, 115.828, 90.00, 90.00, 120.00
R / Rfree (%)	23.4 / 26.8

The binding sites of Iron atom in the Murine Inos Dimer with Inhibitor 4-Map Bound (pdb code 3e67). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Murine Inos Dimer with Inhibitor 4-Map Bound, PDB code: 3e67:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Murine Inos Dimer with Inhibitor 4-Map Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inos Dimer with Inhibitor 4-Map Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:33.1 occ:1.00 FE A:HEM901 0.0 33.1 1.0 NC A:HEM901 2.0 32.0 1.0 ND A:HEM901 2.0 35.5 1.0 NB A:HEM901 2.0 32.5 1.0 NA A:HEM901 2.1 35.8 1.0 SG A:CYS194 2.3 41.9 1.0 C4C A:HEM901 3.0 33.1 1.0 C1D A:HEM901 3.0 34.9 1.0 C1C A:HEM901 3.0 32.1 1.0 C4D A:HEM901 3.1 35.7 1.0 C4B A:HEM901 3.1 31.8 1.0 C1A A:HEM901 3.1 37.5 1.0 C1B A:HEM901 3.1 31.7 1.0 C4A A:HEM901 3.1 34.6 1.0 CB A:CYS194 3.2 38.7 1.0 CHD A:HEM901 3.4 32.1 1.0 CHC A:HEM901 3.4 30.9 1.0 CHA A:HEM901 3.4 36.4 1.0 CHB A:HEM901 3.5 32.7 1.0 C3 A:BVF904 3.7 33.8 1.0 C4 A:BVF904 3.8 34.5 1.0 C8 A:BVF904 4.0 32.8 1.0 CA A:CYS194 4.0 39.3 1.0 C2 A:BVF904 4.1 33.1 1.0 C3D A:HEM901 4.2 34.8 1.0 C2D A:HEM901 4.3 34.2 1.0 C2C A:HEM901 4.3 32.7 1.0 C3C A:HEM901 4.3 33.3 1.0 C2B A:HEM901 4.3 31.4 1.0 C3B A:HEM901 4.3 30.3 1.0 C5 A:BVF904 4.3 36.9 1.0 C3A A:HEM901 4.3 35.7 1.0 C2A A:HEM901 4.3 37.4 1.0 NE1 A:TRP188 4.5 40.5 1.0 C1 A:BVF904 4.6 32.8 1.0 N6 A:BVF904 4.7 35.1 1.0 N A:ILE195 4.7 40.8 1.0 C A:CYS194 4.8 40.3 1.0 N A:GLY196 4.9 38.8 1.0 N7 A:BVF904 5.0 37.2 1.0

Iron binding site 2 out of 2 in the Murine Inos Dimer with Inhibitor 4-Map Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Murine Inos Dimer with Inhibitor 4-Map Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:38.1 occ:1.00 FE B:HEM901 0.0 38.1 1.0 NB B:HEM901 2.0 33.0 1.0 NA B:HEM901 2.0 33.1 1.0 ND B:HEM901 2.0 32.9 1.0 NC B:HEM901 2.1 31.6 1.0 SG B:CYS194 2.3 40.6 1.0 C1B B:HEM901 3.0 33.5 1.0 C1C B:HEM901 3.0 32.1 1.0 C4B B:HEM901 3.1 33.3 1.0 C4A B:HEM901 3.1 32.8 1.0 C1D B:HEM901 3.1 32.9 1.0 C4D B:HEM901 3.1 34.2 1.0 C1A B:HEM901 3.1 34.1 1.0 C4C B:HEM901 3.1 32.8 1.0 CHC B:HEM901 3.4 34.0 1.0 CB B:CYS194 3.4 39.2 1.0 CHB B:HEM901 3.4 31.9 1.0 CHA B:HEM901 3.4 34.5 1.0 CHD B:HEM901 3.5 32.0 1.0 C3 B:BVF905 3.6 32.5 1.0 C4 B:BVF905 3.8 33.0 1.0 C8 B:BVF905 3.8 29.3 1.0 C2 B:BVF905 4.1 32.1 1.0 CA B:CYS194 4.1 40.7 1.0 C2B B:HEM901 4.2 34.8 1.0 C3B B:HEM901 4.3 34.6 1.0 C3A B:HEM901 4.3 32.6 1.0 C3D B:HEM901 4.3 33.9 1.0 C2D B:HEM901 4.3 33.8 1.0 C2C B:HEM901 4.3 31.2 1.0 C2A B:HEM901 4.3 33.8 1.0 C3C B:HEM901 4.3 31.7 1.0 C5 B:BVF905 4.4 35.4 1.0 NE1 B:TRP188 4.4 36.1 1.0 C1 B:BVF905 4.6 34.8 1.0 N6 B:BVF905 4.8 36.0 1.0 N B:ILE195 4.8 40.0 1.0 C B:CYS194 4.9 40.9 1.0 N B:GLY196 5.0 38.6 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