Iron in PDB 1m9m: Human Endothelial Nitric Oxide Synthase with 6- Nitroindazole Bound

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

The structure of Human Endothelial Nitric Oxide Synthase with 6- Nitroindazole Bound, PDB code: 1m9m 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)	45.03 / 1.96
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	69.757, 90.782, 155.551, 90.00, 90.00, 90.00
R / Rfree (%)	19.3 / 22.3

The structure of Human Endothelial Nitric Oxide Synthase with 6- Nitroindazole Bound also contains other interesting chemical elements:

Zinc	(Zn)	1 atom
Sodium	(Na)	1 atom

The binding sites of Iron atom in the Human Endothelial Nitric Oxide Synthase with 6- Nitroindazole Bound (pdb code 1m9m). 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 6- Nitroindazole Bound, PDB code: 1m9m:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Endothelial 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 Human Endothelial Nitric Oxide Synthase with 6- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:31.1 occ:1.00 FE A:HEM901 0.0 31.1 1.0 ND A:HEM901 2.0 30.0 1.0 NB A:HEM901 2.1 31.4 1.0 NC A:HEM901 2.1 31.2 1.0 NA A:HEM901 2.1 31.6 1.0 SG A:CYS184 2.3 29.7 1.0 C4D A:HEM901 3.1 32.5 1.0 C1B A:HEM901 3.1 30.4 1.0 C4A A:HEM901 3.1 30.5 1.0 C1D A:HEM901 3.1 30.2 1.0 C1C A:HEM901 3.1 32.0 1.0 C4C A:HEM901 3.1 32.0 1.0 C4B A:HEM901 3.1 31.1 1.0 C1A A:HEM901 3.1 31.9 1.0 O11 A:6NI906 3.3 55.8 0.0 CB A:CYS184 3.3 29.6 1.0 CHB A:HEM901 3.4 29.7 1.0 CHC A:HEM901 3.4 30.1 1.0 CHA A:HEM901 3.4 30.6 1.0 N10 A:6NI906 3.5 55.7 1.0 CHD A:HEM901 3.5 30.3 1.0 C6 A:6NI906 3.6 53.6 1.0 C7 A:6NI906 3.9 51.5 1.0 CA A:CYS184 4.1 30.8 1.0 O12 A:6NI906 4.2 55.6 1.0 C5 A:6NI906 4.2 52.4 1.0 C3D A:HEM901 4.3 31.5 1.0 C2D A:HEM901 4.3 29.9 1.0 C2B A:HEM901 4.3 31.4 1.0 C3A A:HEM901 4.3 32.6 1.0 C3B A:HEM901 4.3 31.9 1.0 C3C A:HEM901 4.3 32.3 1.0 C2C A:HEM901 4.3 31.0 1.0 C2A A:HEM901 4.3 34.0 1.0 NE1 A:TRP178 4.4 28.7 1.0 C8 A:6NI906 4.7 49.9 1.0 C A:CYS184 4.9 30.7 1.0 N A:GLY186 5.0 30.9 1.0 CD1 A:TRP178 5.0 28.8 1.0

Iron binding site 2 out of 2 in the Human Endothelial 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 Human Endothelial Nitric Oxide Synthase with 6- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:30.4 occ:1.00 FE B:HEM901 0.0 30.4 1.0 ND B:HEM901 2.1 29.8 1.0 NB B:HEM901 2.1 31.2 1.0 NA B:HEM901 2.1 31.6 1.0 NC B:HEM901 2.1 29.1 1.0 SG B:CYS184 2.4 28.9 1.0 C1D B:HEM901 3.1 31.7 1.0 C1B B:HEM901 3.1 30.8 1.0 C4A B:HEM901 3.1 32.1 1.0 C4D B:HEM901 3.1 34.1 1.0 C4C B:HEM901 3.1 28.2 1.0 C1A B:HEM901 3.1 31.7 1.0 C1C B:HEM901 3.1 29.7 1.0 C4B B:HEM901 3.1 30.9 1.0 O12 B:6NI907 3.2 61.2 0.0 CB B:CYS184 3.3 27.5 1.0 CHB B:HEM901 3.4 30.8 1.0 CHA B:HEM901 3.4 32.1 1.0 CHC B:HEM901 3.4 30.6 1.0 CHD B:HEM901 3.4 29.3 1.0 N10 B:6NI907 3.7 61.7 1.0 C6 B:6NI907 3.8 59.4 1.0 C7 B:6NI907 4.0 57.5 1.0 CA B:CYS184 4.1 26.8 1.0 C2D B:HEM901 4.3 32.7 1.0 C3A B:HEM901 4.3 33.6 1.0 C3D B:HEM901 4.3 36.0 1.0 C2B B:HEM901 4.3 30.4 1.0 C2A B:HEM901 4.3 34.6 1.0 C3C B:HEM901 4.3 29.6 1.0 C2C B:HEM901 4.3 29.3 1.0 C3B B:HEM901 4.3 31.2 1.0 C5 B:6NI907 4.4 58.3 1.0 NE1 B:TRP178 4.4 25.8 1.0 C8 B:6NI907 4.7 56.4 1.0 O11 B:6NI907 4.8 61.7 1.0 C B:CYS184 4.9 28.5 1.0 N B:GLY186 4.9 26.3 1.0 N B:VAL185 4.9 27.1 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