Iron in PDB 1n2n: Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase.

All present enzymatic activity of Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase.:
1.14.13.39;

The structure of Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase., PDB code: 1n2n was solved by R.Fedorov, D.K.Ghosh, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.40
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	214.800, 214.800, 117.600, 90.00, 90.00, 120.00
R / Rfree (%)	20.6 / 24.3

The structure of Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase. also contains other interesting chemical elements:

Zinc

(Zn)

2 atoms

The binding sites of Iron atom in the Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase. (pdb code 1n2n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase., PDB code: 1n2n:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase. within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe900 b:36.6 occ:1.00 FE A:HEM900 0.0 36.6 1.0 C A:CYN903 1.9 38.9 1.0 NB A:HEM900 2.0 34.0 1.0 NA A:HEM900 2.0 33.9 1.0 ND A:HEM900 2.0 35.8 1.0 NC A:HEM900 2.0 35.5 1.0 SG A:CYS194 2.4 36.0 1.0 C1B A:HEM900 3.0 33.6 1.0 C4B A:HEM900 3.0 34.9 1.0 C4A A:HEM900 3.0 35.0 1.0 C1A A:HEM900 3.0 33.6 1.0 C1D A:HEM900 3.0 36.7 1.0 C1C A:HEM900 3.0 34.7 1.0 C4D A:HEM900 3.1 35.2 1.0 C4C A:HEM900 3.1 36.8 1.0 N A:CYN903 3.1 40.7 1.0 CHB A:HEM900 3.4 34.0 1.0 CHC A:HEM900 3.4 35.6 1.0 CHA A:HEM900 3.4 34.8 1.0 CHD A:HEM900 3.4 36.1 1.0 CB A:CYS194 3.4 33.5 1.0 CA A:CYS194 4.1 33.2 1.0 C2B A:HEM900 4.2 32.0 1.0 C3B A:HEM900 4.2 32.8 1.0 C2A A:HEM900 4.3 34.0 1.0 C3A A:HEM900 4.3 34.8 1.0 C3D A:HEM900 4.3 35.3 1.0 C2D A:HEM900 4.3 36.5 1.0 C2C A:HEM900 4.3 36.9 1.0 C3C A:HEM900 4.3 36.2 1.0 NH1 A:ARG902 4.4 46.6 1.0 NE1 A:TRP188 4.4 32.4 1.0 CZ A:ARG902 4.8 50.8 1.0 C A:CYS194 4.9 32.9 1.0 N A:ILE195 4.9 33.0 1.0 N A:GLY196 4.9 37.0 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Cyanide Complex of the Oxygenase Domain of Inducible Nitric Oxide Synthase. within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe900 b:37.6 occ:1.00 FE B:HEM900 0.0 37.6 1.0 ND B:HEM900 1.9 35.6 1.0 NC B:HEM900 2.0 36.2 1.0 NB B:HEM900 2.0 35.0 1.0 NA B:HEM900 2.0 35.7 1.0 SG B:CYS194 2.5 36.5 1.0 C1D B:HEM900 3.0 35.8 1.0 C1C B:HEM900 3.0 35.9 1.0 C4B B:HEM900 3.0 34.9 1.0 C4C B:HEM900 3.0 35.8 1.0 C4D B:HEM900 3.0 36.5 1.0 C1B B:HEM900 3.0 35.0 1.0 C4A B:HEM900 3.1 35.3 1.0 C1A B:HEM900 3.1 36.5 1.0 O B:HOH2165 3.1 48.1 1.0 CHC B:HEM900 3.3 34.9 1.0 CHD B:HEM900 3.4 35.4 1.0 CHB B:HEM900 3.4 35.6 1.0 CB B:CYS194 3.4 34.5 1.0 CHA B:HEM900 3.4 35.7 1.0 NH1 B:ARG1902 4.2 54.4 1.0 CA B:CYS194 4.2 34.5 1.0 C2D B:HEM900 4.2 35.8 1.0 C2C B:HEM900 4.2 36.3 1.0 C3D B:HEM900 4.3 36.2 1.0 C3C B:HEM900 4.3 36.1 1.0 C2B B:HEM900 4.3 33.9 1.0 C3B B:HEM900 4.3 32.8 1.0 C3A B:HEM900 4.3 35.8 1.0 C2A B:HEM900 4.3 35.4 1.0 NE1 B:TRP188 4.5 31.1 1.0 CZ B:ARG1902 4.8 53.5 1.0 C B:CYS194 5.0 35.6 1.0

R.Fedorov, D.K.Ghosh, I.Schlichting. Crystal Structures of Cyanide Complexes of P450CAM and the Oxygenase Domain of Inducible Nitric Oxide Synthase-Structural Models of the Short-Lived Oxygen Complexes Arch.Biochem.Biophys. V. 409 25 2003.
ISSN: ISSN 0003-9861
PubMed: 12464241
DOI: 10.1016/S0003-9861(02)00555-6