Iron in PDB 1qw5: Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor.

All present enzymatic activity of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor.:
1.14.13.39;

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor., PDB code: 1qw5 was solved by R.Fedorov, E.Hartmann, D.K.Ghosh, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.70
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	214.561, 214.561, 117.391, 90.00, 90.00, 120.00
R / Rfree (%)	21.1 / 26.4

The structure of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor. also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor. (pdb code 1qw5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor., PDB code: 1qw5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe900 b:43.2 occ:1.00 FE A:HEM900 0.0 43.2 1.0 ND A:HEM900 1.9 44.9 1.0 NA A:HEM900 2.0 42.5 1.0 NC A:HEM900 2.0 55.7 1.0 NB A:HEM900 2.1 45.1 1.0 SG A:CYS194 2.4 42.0 1.0 C4D A:HEM900 3.0 48.1 1.0 C1D A:HEM900 3.0 41.4 1.0 C1A A:HEM900 3.0 45.3 1.0 C4C A:HEM900 3.0 53.6 1.0 C1C A:HEM900 3.1 51.3 1.0 C4A A:HEM900 3.1 42.4 1.0 C4B A:HEM900 3.1 42.4 1.0 C1B A:HEM900 3.1 45.2 1.0 CHA A:HEM900 3.4 47.6 1.0 CHD A:HEM900 3.4 43.5 1.0 CHC A:HEM900 3.4 44.0 1.0 CHB A:HEM900 3.5 41.7 1.0 CB A:CYS194 3.5 43.3 1.0 C10 A:14W902 4.1 37.4 1.0 CA A:CYS194 4.1 37.1 1.0 C3D A:HEM900 4.2 41.0 1.0 C2D A:HEM900 4.2 37.5 1.0 C2A A:HEM900 4.3 39.7 1.0 C9 A:14W902 4.3 38.5 1.0 C2C A:HEM900 4.3 55.2 1.0 C3A A:HEM900 4.3 44.8 1.0 C3C A:HEM900 4.3 57.2 1.0 C2B A:HEM900 4.4 46.0 1.0 C3B A:HEM900 4.4 42.6 1.0 C7 A:14W902 4.4 37.5 1.0 N8 A:14W902 4.6 38.2 1.0 NE1 A:TRP188 4.7 42.6 1.0 N11 A:14W902 4.8 39.1 1.0 C A:CYS194 4.9 38.6 1.0 N A:ILE195 4.9 38.5 1.0

Iron binding site 2 out of 2 in the Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Murine Inducible Nitric Oxide Synthase Oxygenase Domain in Complex with W1400 Inhibitor. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe900 b:43.0 occ:1.00 FE B:HEM900 0.0 43.0 1.0 ND B:HEM900 1.9 42.5 1.0 NC B:HEM900 2.0 48.5 1.0 NA B:HEM900 2.0 43.8 1.0 NB B:HEM900 2.1 42.8 1.0 SG B:CYS194 2.3 38.2 1.0 C4D B:HEM900 2.9 44.0 1.0 C1D B:HEM900 2.9 44.4 1.0 C1C B:HEM900 3.0 45.9 1.0 C4C B:HEM900 3.0 46.6 1.0 C1A B:HEM900 3.1 42.5 1.0 C4A B:HEM900 3.1 38.4 1.0 C4B B:HEM900 3.1 46.2 1.0 C1B B:HEM900 3.2 43.3 1.0 CHD B:HEM900 3.3 46.2 1.0 CB B:CYS194 3.4 38.8 1.0 CHA B:HEM900 3.4 44.1 1.0 CHC B:HEM900 3.4 47.9 1.0 CHB B:HEM900 3.5 40.2 1.0 C10 B:14W904 3.9 38.5 1.0 CA B:CYS194 4.1 32.8 1.0 C2D B:HEM900 4.2 39.6 1.0 C3D B:HEM900 4.2 35.0 1.0 C3C B:HEM900 4.3 45.7 1.0 C2A B:HEM900 4.3 37.6 1.0 C2C B:HEM900 4.3 47.1 1.0 C3A B:HEM900 4.3 39.2 1.0 C2B B:HEM900 4.4 45.1 1.0 C9 B:14W904 4.4 39.3 1.0 C3B B:HEM900 4.4 42.4 1.0 C7 B:14W904 4.5 40.8 1.0 NE1 B:TRP188 4.5 41.0 1.0 N8 B:14W904 4.7 40.3 1.0 C B:CYS194 4.8 34.7 1.0 N B:ILE195 5.0 35.0 1.0

R.Fedorov, E.Hartmann, D.K.Ghosh, I.Schlichting. Structural Basis For the Specificity of the Nitric-Oxide Synthase Inhibitors W1400 and Nomega-Propyl-L-Arg For the Inducible and Neuronal Isoforms. J.Biol.Chem. V. 278 45818 2003.
ISSN: ISSN 0021-9258
PubMed: 12954642
DOI: 10.1074/JBC.M306030200