Iron in PDB 2hx4: Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide

All present enzymatic activity of Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide:
1.14.13.39;

The structure of Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide, PDB code: 2hx4 was solved by J.Igarashi, H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.51 / 2.15
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.920, 111.000, 164.350, 90.00, 90.00, 90.00
R / Rfree (%)	20.3 / 24.5

The structure of Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide (pdb code 2hx4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide, PDB code: 2hx4:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe750 b:23.2 occ:1.00 FE A:HEM750 0.0 23.2 1.0 ND A:HEM750 2.0 24.9 1.0 NC A:HEM750 2.0 21.2 1.0 NB A:HEM750 2.0 24.7 1.0 NA A:HEM750 2.0 24.9 1.0 SG A:CYS415 2.3 23.6 1.0 C4C A:HEM750 3.0 21.6 1.0 C4D A:HEM750 3.1 25.4 1.0 C1C A:HEM750 3.1 22.2 1.0 C1D A:HEM750 3.1 24.4 1.0 C1A A:HEM750 3.1 25.4 1.0 C4B A:HEM750 3.1 25.4 1.0 C4A A:HEM750 3.1 24.6 1.0 C1B A:HEM750 3.1 23.7 1.0 CB A:CYS415 3.4 23.9 1.0 CHD A:HEM750 3.4 24.4 1.0 CHA A:HEM750 3.5 22.9 1.0 CHC A:HEM750 3.5 22.8 1.0 CHB A:HEM750 3.5 23.4 1.0 NH1 A:4HX799 4.0 29.5 1.0 CA A:CYS415 4.1 22.3 1.0 C3C A:HEM750 4.3 22.9 1.0 C3D A:HEM750 4.3 25.1 1.0 C2C A:HEM750 4.3 22.9 1.0 C2D A:HEM750 4.3 25.3 1.0 C2A A:HEM750 4.3 23.8 1.0 C3A A:HEM750 4.3 25.3 1.0 C3B A:HEM750 4.3 26.7 1.0 C2B A:HEM750 4.4 24.7 1.0 NO A:4HX799 4.4 30.4 1.0 CZ A:4HX799 4.4 32.9 1.0 NE1 A:TRP409 4.5 25.1 1.0 NH2 A:4HX799 4.8 29.3 1.0 O3 A:4HX799 4.8 27.5 1.0 O2 A:4HX799 4.8 30.9 1.0 C A:CYS415 4.8 20.9 1.0 N A:GLY417 4.9 22.5 1.0 N A:VAL416 4.9 20.5 1.0

Iron binding site 2 out of 2 in the Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe750 b:22.2 occ:1.00 FE B:HEM750 0.0 22.2 1.0 NC B:HEM750 2.0 20.5 1.0 NA B:HEM750 2.0 24.0 1.0 NB B:HEM750 2.0 21.9 1.0 ND B:HEM750 2.0 22.0 1.0 SG B:CYS415 2.3 22.9 1.0 C4C B:HEM750 3.0 20.8 1.0 C1C B:HEM750 3.0 19.6 1.0 C1D B:HEM750 3.0 21.7 1.0 C1A B:HEM750 3.0 23.8 1.0 C4B B:HEM750 3.1 22.9 1.0 C4D B:HEM750 3.1 22.7 1.0 C1B B:HEM750 3.1 22.8 1.0 C4A B:HEM750 3.1 22.8 1.0 CB B:CYS415 3.4 19.9 1.0 CHD B:HEM750 3.4 20.3 1.0 CHC B:HEM750 3.4 19.4 1.0 CHA B:HEM750 3.5 21.7 1.0 CHB B:HEM750 3.5 23.9 1.0 NH1 B:4HX799 4.0 30.0 1.0 CA B:CYS415 4.2 21.1 1.0 C3C B:HEM750 4.2 21.1 1.0 C2C B:HEM750 4.3 20.7 1.0 C2A B:HEM750 4.3 25.0 1.0 C2D B:HEM750 4.3 21.6 1.0 C3D B:HEM750 4.3 24.0 1.0 C3A B:HEM750 4.3 22.9 1.0 C3B B:HEM750 4.3 25.6 1.0 C2B B:HEM750 4.3 21.8 1.0 CZ B:4HX799 4.4 29.9 1.0 NO B:4HX799 4.4 29.6 1.0 NE1 B:TRP409 4.5 20.2 1.0 O2 B:4HX799 4.7 32.0 1.0 N B:GLY417 4.8 23.9 1.0 NH2 B:4HX799 4.8 25.9 1.0 C B:CYS415 4.9 22.0 1.0 NE B:4HX799 4.9 30.4 1.0 N B:VAL416 4.9 21.6 1.0 O3 B:4HX799 4.9 30.6 1.0

J.Seo, J.Igarashi, H.Li, P.Martasek, L.J.Roman, T.L.Poulos, R.B.Silverman. Structure-Based Design and Synthesis of N(Omega)-Nitro-L-Arginine-Containing Peptidomimetics As Selective Inhibitors of Neuronal Nitric Oxide Synthase. Displacement of the Heme Structural Water. J.Med.Chem. V. 50 2089 2007.
ISSN: ISSN 0022-2623
PubMed: 17425297
DOI: 10.1021/JM061305C