Iron in PDB 1vaf: Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477

All present enzymatic activity of Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477:
1.14.13.39;

The structure of Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477, PDB code: 1vaf was solved by R.Fedorov, R.Vasan, 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 / 2.90
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	216.344, 216.344, 117.835, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / 26.2

The structure of Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 also contains other interesting chemical elements:

Chlorine	(Cl)	4 atoms
Zinc	(Zn)	2 atoms

The binding sites of Iron atom in the Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 (pdb code 1vaf). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477, PDB code: 1vaf:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe900 b:46.0 occ:1.00 FE A:HEM900 0.0 46.0 1.0 NC A:HEM900 1.9 46.4 1.0 NB A:HEM900 1.9 45.2 1.0 ND A:HEM900 2.0 46.1 1.0 NA A:HEM900 2.1 43.7 1.0 SG A:CYS194 2.3 47.1 1.0 C1C A:HEM900 2.9 46.2 1.0 C4B A:HEM900 3.0 45.0 1.0 C4C A:HEM900 3.0 47.7 1.0 C4D A:HEM900 3.0 45.7 1.0 C1D A:HEM900 3.0 46.8 1.0 C1B A:HEM900 3.0 44.4 1.0 C1A A:HEM900 3.1 44.1 1.0 C4A A:HEM900 3.1 44.2 1.0 CHC A:HEM900 3.3 45.6 1.0 CHD A:HEM900 3.4 47.5 1.0 CHA A:HEM900 3.4 45.1 1.0 CHB A:HEM900 3.5 43.9 1.0 CB A:CYS194 3.6 47.5 1.0 C2C A:HEM900 4.2 47.0 1.0 CA A:CYS194 4.2 47.8 1.0 C3B A:HEM900 4.2 44.5 1.0 C2B A:HEM900 4.2 44.4 1.0 C3C A:HEM900 4.3 47.6 1.0 C3D A:HEM900 4.3 44.9 1.0 C2D A:HEM900 4.3 46.2 1.0 S A:ARR902 4.3 46.8 0.5 S A:ARR902 4.3 46.8 0.5 C3A A:HEM900 4.3 44.5 1.0 C2A A:HEM900 4.4 44.5 1.0 C4 A:ARR902 4.5 41.7 0.5 C4 A:ARR902 4.5 41.7 0.5 NE1 A:TRP188 4.6 43.0 1.0 C1 A:ARR902 4.6 40.6 0.5 C1 A:ARR902 4.6 40.6 0.5 C3 A:ARR902 4.8 42.5 0.5 C3 A:ARR902 4.8 42.5 0.5 C5 A:ARR902 4.8 49.4 0.5 C5 A:ARR902 4.8 49.4 0.5 N3 A:ARR902 4.9 44.9 0.5 N3 A:ARR902 4.9 44.9 0.5 C2 A:ARR902 4.9 43.4 0.5 C2 A:ARR902 4.9 43.4 0.5 N A:ILE195 4.9 49.8 1.0 C A:CYS194 5.0 48.8 1.0 N A:GLY196 5.0 50.6 1.0

Iron binding site 2 out of 2 in the Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Inducible Nitric Oxide Synthase Oxygenase Domain Complexed with the Inhibitor Ar-R17477 within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe900 b:52.6 occ:1.00 FE B:HEM900 0.0 52.6 1.0 NC B:HEM900 1.9 52.2 1.0 ND B:HEM900 2.0 51.7 1.0 NB B:HEM900 2.0 51.4 1.0 NA B:HEM900 2.0 50.0 1.0 SG B:CYS194 2.6 51.8 1.0 C1C B:HEM900 3.0 51.8 1.0 C4C B:HEM900 3.0 51.8 1.0 C1D B:HEM900 3.0 51.7 1.0 C4D B:HEM900 3.0 51.1 1.0 C4B B:HEM900 3.1 50.5 1.0 C1A B:HEM900 3.1 50.8 1.0 C1B B:HEM900 3.1 50.6 1.0 C4A B:HEM900 3.1 49.5 1.0 CHD B:HEM900 3.4 51.7 1.0 CB B:CYS194 3.4 52.7 1.0 CHC B:HEM900 3.4 50.7 1.0 CHA B:HEM900 3.4 50.9 1.0 CHB B:HEM900 3.5 48.8 1.0 CA B:CYS194 4.1 53.4 1.0 S B:ARR903 4.2 56.8 0.5 S B:ARR903 4.2 56.8 0.5 C2C B:HEM900 4.2 52.3 1.0 C2D B:HEM900 4.3 51.2 1.0 C3C B:HEM900 4.3 51.4 1.0 C3D B:HEM900 4.3 50.7 1.0 C3B B:HEM900 4.3 50.4 1.0 C2B B:HEM900 4.3 50.4 1.0 C3A B:HEM900 4.3 49.6 1.0 C2A B:HEM900 4.3 50.0 1.0 C4 B:ARR903 4.5 41.7 0.5 C4 B:ARR903 4.5 41.7 0.5 C1 B:ARR903 4.5 50.6 0.5 C1 B:ARR903 4.5 50.6 0.5 NE1 B:TRP188 4.6 54.5 1.0 C3 B:ARR903 4.8 42.5 0.5 C3 B:ARR903 4.8 52.5 0.5 N3 B:ARR903 4.8 54.9 0.5 N3 B:ARR903 4.8 44.9 0.5 C5 B:ARR903 4.8 59.4 0.5 C5 B:ARR903 4.8 49.4 0.5 C B:CYS194 4.8 53.0 1.0 C2 B:ARR903 4.9 53.4 0.5 C2 B:ARR903 4.9 43.4 0.5 N B:ILE195 4.9 52.7 1.0 N B:GLY196 5.0 49.8 1.0

R.Fedorov, R.Vasan, D.K.Ghosh, I.Schlichting. Structures of Nitric Oxide Synthase Isoforms Complexed with the Inhibitor Ar-R17477 Suggest A Rational Basis For Specificity and Inhibitor Design Proc.Natl.Acad.Sci.Usa V. 101 5892 2004.
ISSN: ISSN 0027-8424
PubMed: 15071192
DOI: 10.1073/PNAS.0306588101