Iron in PDB 4fvy: Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine

All present enzymatic activity of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine:
1.14.13.39;

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine, PDB code: 4fvy was solved by H.Li, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.89 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.889, 110.937, 164.468, 90.00, 90.00, 90.00
R / Rfree (%)	18.4 / 21.2

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Iron atom in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine (pdb code 4fvy). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine, PDB code: 4fvy:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:21.3 occ:1.00 FE A:HEM801 0.0 21.3 1.0 NA A:HEM801 2.0 22.5 1.0 NB A:HEM801 2.0 23.0 1.0 ND A:HEM801 2.1 22.2 1.0 NC A:HEM801 2.1 20.8 1.0 SG A:CYS415 2.5 20.5 1.0 C4A A:HEM801 3.0 22.9 1.0 C1A A:HEM801 3.0 21.7 1.0 C1B A:HEM801 3.1 21.9 1.0 C1D A:HEM801 3.1 19.9 1.0 C1C A:HEM801 3.1 20.8 1.0 C4D A:HEM801 3.1 21.9 1.0 C4B A:HEM801 3.1 21.6 1.0 C4C A:HEM801 3.1 20.9 1.0 CHB A:HEM801 3.4 20.5 1.0 CB A:CYS415 3.4 19.5 1.0 CHA A:HEM801 3.4 23.3 1.0 CHD A:HEM801 3.4 20.8 1.0 CHC A:HEM801 3.4 21.4 1.0 C1 A:3KJ804 3.5 23.9 1.0 CA A:CYS415 4.2 19.2 1.0 C3A A:HEM801 4.3 21.0 1.0 C2A A:HEM801 4.3 21.6 1.0 C2B A:HEM801 4.3 23.5 1.0 C3C A:HEM801 4.3 19.8 1.0 C2D A:HEM801 4.3 21.3 1.0 C3B A:HEM801 4.3 23.5 1.0 C2C A:HEM801 4.3 20.3 1.0 C3D A:HEM801 4.3 21.8 1.0 NH2 A:3KJ804 4.3 23.4 1.0 NE1 A:TRP409 4.4 20.6 1.0 OH A:3KJ804 4.6 27.8 1.0 CZ A:3KJ804 4.7 23.9 1.0 N A:GLY417 4.8 19.2 1.0 C A:CYS415 4.9 19.1 1.0

Iron binding site 2 out of 2 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Hydroxy- N(Omega)-Methyl-L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:20.1 occ:1.00 FE B:HEM801 0.0 20.1 1.0 NB B:HEM801 2.0 19.3 1.0 ND B:HEM801 2.0 19.7 1.0 NC B:HEM801 2.1 20.9 1.0 NA B:HEM801 2.1 21.8 1.0 SG B:CYS415 2.5 18.9 1.0 C4B B:HEM801 3.0 20.6 1.0 C1B B:HEM801 3.1 21.6 1.0 C1D B:HEM801 3.1 22.9 1.0 C4C B:HEM801 3.1 18.3 1.0 C1A B:HEM801 3.1 18.5 1.0 C4D B:HEM801 3.1 19.7 1.0 C1C B:HEM801 3.1 17.5 1.0 C4A B:HEM801 3.1 21.6 1.0 CHC B:HEM801 3.4 18.1 1.0 CHD B:HEM801 3.4 21.1 1.0 CHA B:HEM801 3.4 18.6 1.0 CB B:CYS415 3.4 14.6 1.0 CHB B:HEM801 3.5 19.6 1.0 C1 B:3KJ804 3.5 23.9 1.0 C2B B:HEM801 4.3 22.0 1.0 C3B B:HEM801 4.3 24.9 1.0 CA B:CYS415 4.3 16.1 1.0 C3C B:HEM801 4.3 17.7 1.0 C2D B:HEM801 4.3 20.4 1.0 C2C B:HEM801 4.3 17.9 1.0 C2A B:HEM801 4.3 20.4 1.0 C3D B:HEM801 4.3 21.6 1.0 NH2 B:3KJ804 4.3 22.0 1.0 C3A B:HEM801 4.3 19.9 1.0 NE1 B:TRP409 4.4 19.6 1.0 CZ B:3KJ804 4.6 22.5 1.0 OH B:3KJ804 4.7 27.6 1.0 N B:GLY417 4.8 19.4 1.0 C B:CYS415 4.9 17.5 1.0 NH1 B:3KJ804 5.0 20.3 1.0 N B:VAL416 5.0 17.6 1.0

K.Jansen Labby, H.Li, L.J.Roman, P.Martasek, T.L.Poulos, R.B.Silverman. Methylated N(Omega)-Hydroxy-L-Arginine Analogues As Mechanistic Probes For the Second Step of the Nitric Oxide Synthase-Catalyzed Reaction Biochemistry V. 52 3062 2013.
ISSN: ISSN 0006-2960
PubMed: 23586781
DOI: 10.1021/BI301571V