Iron in PDB 1m9j: Human Endothelial Nitric Oxide Synthase with Chlorzoxazone Bound

All present enzymatic activity of Human Endothelial Nitric Oxide Synthase with Chlorzoxazone Bound:
1.14.13.39;

The structure of Human Endothelial Nitric Oxide Synthase with Chlorzoxazone Bound, PDB code: 1m9j 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)	20.00 / 2.43
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	71.071, 89.891, 155.833, 90.00, 90.00, 90.00
R / Rfree (%)	21.6 / 27.2

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

Chlorine	(Cl)	2 atoms
Zinc	(Zn)	1 atom

The binding sites of Iron atom in the Human Endothelial Nitric Oxide Synthase with Chlorzoxazone Bound (pdb code 1m9j). 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 Chlorzoxazone Bound, PDB code: 1m9j:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Human Endothelial Nitric Oxide Synthase with Chlorzoxazone 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 Chlorzoxazone Bound within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe901 b:35.8 occ:1.00 FE A:HEM901 0.0 35.8 1.0 NB A:HEM901 2.0 34.1 1.0 ND A:HEM901 2.0 36.9 1.0 NA A:HEM901 2.1 35.9 1.0 NC A:HEM901 2.1 33.2 1.0 SG A:CYS184 2.3 30.6 1.0 C1B A:HEM901 3.0 33.1 1.0 C4A A:HEM901 3.1 35.6 1.0 C4B A:HEM901 3.1 33.3 1.0 C1D A:HEM901 3.1 36.0 1.0 C4D A:HEM901 3.1 38.8 1.0 C1A A:HEM901 3.1 38.4 1.0 C1C A:HEM901 3.1 33.2 1.0 C4C A:HEM901 3.1 31.9 1.0 CHB A:HEM901 3.4 33.4 1.0 CB A:CYS184 3.4 28.0 1.0 CHC A:HEM901 3.4 32.8 1.0 CHA A:HEM901 3.4 38.4 1.0 CHD A:HEM901 3.4 33.6 1.0 C6 A:CLW906 3.9 33.5 1.0 C5 A:CLW906 4.1 33.1 1.0 C1 A:CLW906 4.1 35.4 1.0 CA A:CYS184 4.2 26.5 1.0 C2B A:HEM901 4.3 31.0 1.0 C3A A:HEM901 4.3 38.0 1.0 C3B A:HEM901 4.3 31.5 1.0 C2A A:HEM901 4.3 40.8 1.0 NE1 A:TRP178 4.3 25.9 1.0 C3D A:HEM901 4.3 40.2 1.0 C2D A:HEM901 4.3 38.6 1.0 C3C A:HEM901 4.4 31.2 1.0 C2C A:HEM901 4.4 32.7 1.0 CL1 A:CLW906 4.5 35.5 1.0 C4 A:CLW906 4.5 34.3 1.0 C2 A:CLW906 4.5 34.6 1.0 C3 A:CLW906 4.7 34.4 1.0 C A:CYS184 5.0 26.0 1.0

Iron binding site 2 out of 2 in the Human Endothelial Nitric Oxide Synthase with Chlorzoxazone 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 Chlorzoxazone Bound within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe901 b:33.5 occ:1.00 FE B:HEM901 0.0 33.5 1.0 NB B:HEM901 2.1 35.8 1.0 ND B:HEM901 2.1 36.6 1.0 NA B:HEM901 2.1 37.0 1.0 NC B:HEM901 2.1 34.7 1.0 SG B:CYS184 2.3 32.5 1.0 C4D B:HEM901 3.0 38.2 1.0 C1B B:HEM901 3.1 35.8 1.0 C4B B:HEM901 3.1 36.0 1.0 C1D B:HEM901 3.1 36.2 1.0 C4A B:HEM901 3.1 37.5 1.0 C1A B:HEM901 3.1 38.9 1.0 C4C B:HEM901 3.1 34.5 1.0 C1C B:HEM901 3.1 34.0 1.0 CB B:CYS184 3.3 28.5 1.0 CHA B:HEM901 3.4 39.0 1.0 CHB B:HEM901 3.4 37.1 1.0 CHC B:HEM901 3.4 34.9 1.0 CHD B:HEM901 3.5 36.0 1.0 CA B:CYS184 4.1 29.2 1.0 C6 B:CLW907 4.1 32.9 1.0 C3D B:HEM901 4.2 41.1 1.0 C2D B:HEM901 4.3 37.6 1.0 C3A B:HEM901 4.3 39.2 1.0 C2B B:HEM901 4.3 37.5 1.0 C1 B:CLW907 4.3 34.0 1.0 C2A B:HEM901 4.3 42.1 1.0 C3B B:HEM901 4.3 38.1 1.0 C5 B:CLW907 4.4 32.2 1.0 C2C B:HEM901 4.4 34.9 1.0 C3C B:HEM901 4.4 35.0 1.0 NE1 B:TRP178 4.4 35.6 1.0 CL1 B:CLW907 4.5 33.6 1.0 C2 B:CLW907 4.7 31.3 1.0 C4 B:CLW907 4.7 31.8 1.0 C B:CYS184 4.8 28.9 1.0 C3 B:CLW907 4.9 32.1 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