Iron in PDB 1m9q: Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound

All present enzymatic activity of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound:
1.14.13.39;

The structure of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound, PDB code: 1m9q 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)	34.09 / 2.01
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.508, 90.888, 155.789, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 22.6

The structure of Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Human Endothelial Nitric Oxide Synthase with 5- Nitroindazole Bound (pdb code 1m9q). 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 5- Nitroindazole Bound, PDB code: 1m9q:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Endothelial Nitric Oxide Synthase with 5- 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 5- 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 NC A:HEM901 2.1 31.1 1.0 ND A:HEM901 2.1 30.5 1.0 NA A:HEM901 2.1 31.2 1.0 NB A:HEM901 2.1 29.4 1.0 SG A:CYS184 2.3 29.2 1.0 C4D A:HEM901 3.1 32.8 1.0 C1C A:HEM901 3.1 30.5 1.0 C1A A:HEM901 3.1 33.3 1.0 C4C A:HEM901 3.1 32.5 1.0 C4B A:HEM901 3.1 29.7 1.0 C1D A:HEM901 3.1 30.6 1.0 C1B A:HEM901 3.1 30.1 1.0 C4A A:HEM901 3.1 31.9 1.0 CB A:CYS184 3.4 27.2 1.0 CHC A:HEM901 3.4 29.9 1.0 CHA A:HEM901 3.4 29.3 1.0 CHB A:HEM901 3.5 29.0 1.0 CHD A:HEM901 3.5 31.2 1.0 C6 A:5NI907 3.9 77.2 0.8 C5 A:5NI907 4.0 77.8 0.8 N10 A:5NI907 4.1 79.5 0.8 CA A:CYS184 4.1 28.9 1.0 O11 A:5NI907 4.1 80.2 0.8 C3D A:HEM901 4.3 33.0 1.0 C2D A:HEM901 4.3 30.1 1.0 C2C A:HEM901 4.3 30.4 1.0 C3C A:HEM901 4.3 31.5 1.0 C3A A:HEM901 4.3 33.5 1.0 C2A A:HEM901 4.3 35.4 1.0 C2B A:HEM901 4.3 29.9 1.0 C3B A:HEM901 4.3 31.0 1.0 NE1 A:TRP178 4.4 27.2 1.0 O12 A:5NI907 4.5 80.9 0.8 C7 A:5NI907 4.6 75.9 0.8 C4 A:5NI907 4.8 76.6 0.8 C A:CYS184 4.9 29.0 1.0 N A:GLY186 4.9 30.8 1.0 N A:VAL185 5.0 27.4 1.0 CD1 A:TRP178 5.0 28.0 1.0

Iron binding site 2 out of 2 in the Human Endothelial Nitric Oxide Synthase with 5- 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 5- Nitroindazole Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:30.8 occ:1.00 FE B:HEM901 0.0 30.8 1.0 ND B:HEM901 2.0 30.0 1.0 NA B:HEM901 2.1 33.4 1.0 NC B:HEM901 2.1 27.6 1.0 NB B:HEM901 2.1 29.6 1.0 SG B:CYS184 2.3 28.1 1.0 C1D B:HEM901 3.1 31.3 1.0 C4D B:HEM901 3.1 33.4 1.0 C4A B:HEM901 3.1 32.5 1.0 C1A B:HEM901 3.1 34.9 1.0 C1B B:HEM901 3.1 29.9 1.0 C4C B:HEM901 3.1 26.6 1.0 C1C B:HEM901 3.1 27.7 1.0 C4B B:HEM901 3.1 29.5 1.0 CB B:CYS184 3.3 24.2 1.0 CHD B:HEM901 3.4 29.4 1.0 CHA B:HEM901 3.4 32.3 1.0 CHB B:HEM901 3.4 30.0 1.0 CHC B:HEM901 3.4 29.6 1.0 O11 B:5NI906 3.7 77.5 0.8 N10 B:5NI906 4.0 76.1 0.8 C5 B:5NI906 4.1 75.5 0.8 CA B:CYS184 4.1 27.1 1.0 C6 B:5NI906 4.2 74.5 0.8 C3D B:HEM901 4.3 34.1 1.0 C2D B:HEM901 4.3 32.0 1.0 C3A B:HEM901 4.3 35.3 1.0 C2A B:HEM901 4.3 37.0 1.0 NE1 B:TRP178 4.3 25.1 1.0 C2B B:HEM901 4.3 30.0 1.0 C3C B:HEM901 4.3 28.8 1.0 C3B B:HEM901 4.3 30.6 1.0 C2C B:HEM901 4.4 27.2 1.0 C4 B:5NI906 4.6 74.8 0.8 C B:CYS184 4.8 27.5 1.0 O12 B:5NI906 4.9 76.3 0.8 N B:GLY186 4.9 28.8 1.0 C7 B:5NI906 4.9 74.3 0.8 N B:VAL185 4.9 28.4 1.0 CD1 B:TRP178 5.0 25.1 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