Iron in PDB 1m8h: Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound

All present enzymatic activity of Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound:
1.14.13.39;

The structure of Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound, PDB code: 1m8h was solved by R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, D.J.Stuehr, 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)	19.92 / 2.85
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	213.652, 213.652, 114.521, 90.00, 90.00, 120.00
R / Rfree (%)	24.3 / 29.4

The binding sites of Iron atom in the Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound (pdb code 1m8h). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound, PDB code: 1m8h:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:37.1 occ:1.00 FE A:HEM901 0.0 37.1 1.0 ND A:HEM901 2.0 34.4 1.0 NC A:HEM901 2.0 31.5 1.0 NA A:HEM901 2.0 36.1 1.0 NB A:HEM901 2.1 32.4 1.0 SG A:CYS194 2.3 44.6 1.0 C4D A:HEM901 3.0 34.7 1.0 C1D A:HEM901 3.0 35.0 1.0 C4C A:HEM901 3.0 32.3 1.0 C1C A:HEM901 3.0 31.9 1.0 C1A A:HEM901 3.0 38.4 1.0 C4B A:HEM901 3.1 32.6 1.0 C1B A:HEM901 3.1 32.4 1.0 C4A A:HEM901 3.1 37.1 1.0 CB A:CYS194 3.3 43.5 1.0 CHA A:HEM901 3.3 36.8 1.0 CHD A:HEM901 3.4 33.4 1.0 CHC A:HEM901 3.4 30.4 1.0 CHB A:HEM901 3.5 33.9 1.0 C6 A:6NI906 3.9 51.9 1.0 CA A:CYS194 4.0 44.7 1.0 N10 A:6NI906 4.0 56.1 1.0 O11 A:6NI906 4.1 57.9 1.0 C7 A:6NI906 4.2 50.1 1.0 C3D A:HEM901 4.2 34.4 1.0 NE1 A:TRP188 4.3 45.1 1.0 C5 A:6NI906 4.3 49.3 1.0 C2D A:HEM901 4.3 34.0 1.0 C3C A:HEM901 4.3 30.4 1.0 C2C A:HEM901 4.3 31.2 1.0 C2B A:HEM901 4.3 31.5 1.0 C2A A:HEM901 4.3 39.9 1.0 C3B A:HEM901 4.3 32.6 1.0 C3A A:HEM901 4.3 39.3 1.0 O12 A:6NI906 4.8 61.0 1.0 C A:CYS194 4.8 46.2 1.0 C8 A:6NI906 4.8 48.1 1.0 N A:ILE195 4.8 47.1 1.0 C4 A:6NI906 4.8 48.4 1.0 N A:GLY196 4.8 45.2 1.0

Iron binding site 2 out of 2 in the Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Inducible Nitric Oxide Synthase with 6-Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:38.8 occ:1.00 FE B:HEM901 0.0 38.8 1.0 NA B:HEM901 2.0 38.0 1.0 NB B:HEM901 2.0 35.9 1.0 ND B:HEM901 2.0 38.0 1.0 NC B:HEM901 2.0 38.0 1.0 SG B:CYS194 2.3 44.3 1.0 C1B B:HEM901 3.0 37.4 1.0 C1A B:HEM901 3.0 40.3 1.0 C4A B:HEM901 3.0 39.2 1.0 C4D B:HEM901 3.0 38.7 1.0 C4B B:HEM901 3.0 34.8 1.0 C1C B:HEM901 3.1 37.0 1.0 C1D B:HEM901 3.1 38.9 1.0 C4C B:HEM901 3.1 38.6 1.0 CB B:CYS194 3.2 43.2 1.0 O11 B:6NI907 3.3 58.9 1.0 CHA B:HEM901 3.4 39.3 1.0 CHC B:HEM901 3.4 34.9 1.0 CHB B:HEM901 3.4 37.0 1.0 CHD B:HEM901 3.4 38.8 1.0 N10 B:6NI907 3.8 56.1 1.0 C6 B:6NI907 4.0 54.0 1.0 CA B:CYS194 4.0 45.2 1.0 NE1 B:TRP188 4.1 43.8 1.0 C7 B:6NI907 4.1 51.4 1.0 C2B B:HEM901 4.2 36.8 1.0 C3B B:HEM901 4.3 35.6 1.0 C3A B:HEM901 4.3 40.6 1.0 C2A B:HEM901 4.3 41.9 1.0 C3D B:HEM901 4.3 39.2 1.0 C2C B:HEM901 4.3 36.6 1.0 C2D B:HEM901 4.3 38.8 1.0 C3C B:HEM901 4.3 36.6 1.0 O12 B:6NI907 4.7 60.5 1.0 C5 B:6NI907 4.7 53.1 1.0 N B:ILE195 4.8 46.8 1.0 C B:CYS194 4.8 45.8 1.0 CD1 B:TRP188 4.8 45.0 1.0 N B:GLY196 5.0 44.6 1.0 C8 B:6NI907 5.0 50.2 1.0

R.J.Rosenfeld, E.D.Garcin, K.Panda, G.Andersson, A.Aberg, A.V.Wallace, G.M.Morris, A.J.Olson, D.J.Stuehr, J.A.Tainer, E.D.Getzoff. Conformational Changes in Nitric Oxide Synthases Induced By Chlorzoxazone and Nitroindazoles: Crystallographic and Computational Analyses of Inhibitor Potency Biochemistry V. 41 13915 2002.
ISSN: ISSN 0006-2960
PubMed: 12437348
DOI: 10.1021/BI026313J