Iron in PDB 1m9t: Inducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole Bound

All present enzymatic activity of Inducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole Bound:
1.14.13.39;

The structure of Inducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole Bound, PDB code: 1m9t 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)	19.94 / 2.40
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	214.422, 214.422, 113.267, 90.00, 90.00, 120.00
R / Rfree (%)	25 / 28.4

The structure of Inducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole Bound also contains other interesting chemical elements:

Bromine

(Br)

2 atoms

The binding sites of Iron atom in the Inducible Nitric Oxide Synthase with 3-Bromo-7-Nitroindazole Bound (pdb code 1m9t). 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 3-Bromo-7-Nitroindazole Bound, PDB code: 1m9t:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Inducible Nitric Oxide Synthase with 3-Bromo-7-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 3-Bromo-7-Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:34.2 occ:1.00 FE A:HEM901 0.0 34.2 1.0 NC A:HEM901 2.0 31.7 1.0 NB A:HEM901 2.0 31.0 1.0 ND A:HEM901 2.0 33.1 1.0 NA A:HEM901 2.0 33.5 1.0 SG A:CYS194 2.4 39.3 1.0 C4C A:HEM901 3.0 32.4 1.0 C1B A:HEM901 3.0 31.1 1.0 C1C A:HEM901 3.0 35.1 1.0 C1D A:HEM901 3.1 32.7 1.0 C4A A:HEM901 3.1 33.9 1.0 C4B A:HEM901 3.1 32.0 1.0 C4D A:HEM901 3.1 34.2 1.0 C1A A:HEM901 3.1 36.1 1.0 CB A:CYS194 3.3 38.1 1.0 CHB A:HEM901 3.4 32.2 1.0 CHD A:HEM901 3.4 32.6 1.0 CHC A:HEM901 3.4 34.1 1.0 CHA A:HEM901 3.5 34.6 1.0 CA A:CYS194 4.1 39.3 1.0 C3 A:INE906 4.1 47.5 1.0 N2 A:INE906 4.2 46.4 1.0 C2B A:HEM901 4.3 31.0 1.0 C3C A:HEM901 4.3 31.7 1.0 C3B A:HEM901 4.3 30.3 1.0 C2C A:HEM901 4.3 33.3 1.0 C3A A:HEM901 4.3 35.9 1.0 C2D A:HEM901 4.3 30.3 1.0 C3D A:HEM901 4.3 32.2 1.0 C2A A:HEM901 4.3 38.2 1.0 C9 A:INE906 4.3 44.1 1.0 NE1 A:TRP188 4.4 38.2 1.0 BR A:INE906 4.4 54.7 1.0 N1 A:INE906 4.6 43.2 1.0 C8 A:INE906 4.7 44.4 1.0 N A:GLY196 4.8 37.6 1.0 C A:CYS194 4.8 39.3 1.0 N A:ILE195 4.9 39.2 1.0 C4 A:INE906 5.0 45.5 1.0

Iron binding site 2 out of 2 in the Inducible Nitric Oxide Synthase with 3-Bromo-7-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 3-Bromo-7-Nitroindazole 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 NA B:HEM901 2.0 33.4 1.0 NC B:HEM901 2.0 32.0 1.0 NB B:HEM901 2.0 30.7 1.0 ND B:HEM901 2.0 33.1 1.0 SG B:CYS194 2.4 39.3 1.0 C1B B:HEM901 3.0 29.6 1.0 C4A B:HEM901 3.0 35.6 1.0 C4C B:HEM901 3.0 34.1 1.0 C1D B:HEM901 3.1 32.7 1.0 C1C B:HEM901 3.1 33.6 1.0 C1A B:HEM901 3.1 36.4 1.0 C4B B:HEM901 3.1 31.2 1.0 C4D B:HEM901 3.1 34.0 1.0 CHB B:HEM901 3.3 31.4 1.0 CB B:CYS194 3.4 36.9 1.0 CHD B:HEM901 3.4 33.8 1.0 CHC B:HEM901 3.5 31.8 1.0 CHA B:HEM901 3.5 34.8 1.0 C3 B:INE907 4.0 46.5 1.0 N2 B:INE907 4.1 45.3 1.0 CA B:CYS194 4.1 39.2 1.0 C2B B:HEM901 4.2 29.5 1.0 C3A B:HEM901 4.2 34.6 1.0 C2A B:HEM901 4.3 37.4 1.0 C3B B:HEM901 4.3 28.6 1.0 C3C B:HEM901 4.3 31.4 1.0 C3D B:HEM901 4.3 33.2 1.0 C9 B:INE907 4.3 43.6 1.0 C2C B:HEM901 4.3 31.2 1.0 C2D B:HEM901 4.3 33.7 1.0 NE1 B:TRP188 4.4 34.5 1.0 BR B:INE907 4.4 50.2 1.0 N1 B:INE907 4.5 43.5 1.0 C8 B:INE907 4.6 43.1 1.0 N B:GLY196 4.8 38.3 1.0 C B:CYS194 4.9 39.8 1.0 N B:ILE195 4.9 39.3 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