Iron in PDB 1m9r: Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound

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

The structure of Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound, PDB code: 1m9r 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)	29.65 / 2.56
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.625, 90.280, 155.490, 90.00, 90.00, 90.00
R / Rfree (%)	20.8 / 26.6

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

Bromine	(Br)	4 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound (pdb code 1m9r). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound, PDB code: 1m9r:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Endothelial 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 Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:36.7 occ:1.00 FE A:HEM901 0.0 36.7 1.0 NA A:HEM901 2.0 39.0 1.0 NC A:HEM901 2.1 37.6 1.0 ND A:HEM901 2.1 39.5 1.0 NB A:HEM901 2.1 39.2 1.0 SG A:CYS184 2.3 33.6 1.0 C4D A:HEM901 3.0 40.4 1.0 C1A A:HEM901 3.1 39.9 1.0 C4C A:HEM901 3.1 38.7 1.0 C1C A:HEM901 3.1 37.6 1.0 C1D A:HEM901 3.1 38.9 1.0 C4A A:HEM901 3.1 39.4 1.0 C4B A:HEM901 3.1 38.0 1.0 C1B A:HEM901 3.1 39.6 1.0 CB A:CYS184 3.2 34.6 1.0 CHA A:HEM901 3.4 39.9 1.0 CHD A:HEM901 3.4 40.9 1.0 CHC A:HEM901 3.4 37.6 1.0 CHB A:HEM901 3.5 39.3 1.0 CA A:CYS184 3.9 35.6 1.0 C9 A:INE906 4.0 44.8 1.0 C3 A:INE906 4.2 44.8 1.0 C4 A:INE906 4.2 45.0 1.0 C3D A:HEM901 4.2 40.7 1.0 C2D A:HEM901 4.3 38.9 1.0 NE1 A:TRP178 4.3 40.5 1.0 C2C A:HEM901 4.3 38.5 1.0 C3C A:HEM901 4.3 39.5 1.0 C3A A:HEM901 4.3 39.4 1.0 C2A A:HEM901 4.3 41.8 1.0 C3B A:HEM901 4.3 39.9 1.0 C2B A:HEM901 4.4 39.2 1.0 C8 A:INE906 4.4 44.0 1.0 N2 A:INE906 4.6 45.3 1.0 BR A:INE906 4.7 45.0 1.0 N1 A:INE906 4.7 44.2 1.0 C5 A:INE906 4.8 44.3 1.0 C A:CYS184 4.8 34.9 1.0 CD1 A:TRP178 4.9 39.2 1.0 N A:VAL185 4.9 34.4 1.0 C7 A:INE906 4.9 45.2 1.0

Iron binding site 2 out of 2 in the Human Endothelial 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 Human Endothelial Nitric Oxide Synthase with 3-Bromo-7- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:31.9 occ:1.00 FE B:HEM901 0.0 31.9 1.0 ND B:HEM901 2.0 33.2 1.0 NB B:HEM901 2.1 32.6 1.0 NA B:HEM901 2.1 35.7 1.0 NC B:HEM901 2.1 33.8 1.0 SG B:CYS184 2.3 33.5 1.0 C1D B:HEM901 3.1 34.0 1.0 C4B B:HEM901 3.1 32.2 1.0 C1B B:HEM901 3.1 33.2 1.0 C4D B:HEM901 3.1 36.7 1.0 C4A B:HEM901 3.1 35.2 1.0 C1A B:HEM901 3.1 36.9 1.0 C4C B:HEM901 3.1 33.0 1.0 C1C B:HEM901 3.1 33.5 1.0 CB B:CYS184 3.2 31.3 1.0 CHB B:HEM901 3.4 33.5 1.0 CHD B:HEM901 3.4 35.1 1.0 CHA B:HEM901 3.4 35.7 1.0 CHC B:HEM901 3.4 33.5 1.0 CA B:CYS184 4.0 32.6 1.0 C9 B:INE907 4.1 44.4 1.0 C4 B:INE907 4.3 43.9 1.0 NE1 B:TRP178 4.3 31.5 1.0 C2D B:HEM901 4.3 35.9 1.0 C3B B:HEM901 4.3 31.3 1.0 C3A B:HEM901 4.3 38.4 1.0 C2B B:HEM901 4.3 32.4 1.0 C3 B:INE907 4.3 44.4 1.0 C3D B:HEM901 4.3 39.3 1.0 C2A B:HEM901 4.3 39.6 1.0 C3C B:HEM901 4.4 33.1 1.0 C2C B:HEM901 4.4 33.9 1.0 C8 B:INE907 4.5 43.7 1.0 C5 B:INE907 4.8 46.0 1.0 N2 B:INE907 4.8 42.9 1.0 C B:CYS184 4.8 32.6 1.0 N1 B:INE907 4.8 43.6 1.0 BR B:INE907 4.9 47.7 1.0 C7 B:INE907 4.9 44.6 1.0 N B:VAL185 4.9 32.6 1.0 N B:GLY186 4.9 33.5 1.0 CD1 B:TRP178 5.0 29.7 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