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

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

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-L- Arginine, PDB code: 4fvw 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)	50.00 / 1.81
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	52.149, 111.003, 165.309, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 21.8

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-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)-Methoxy-L- Arginine (pdb code 4fvw). 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)-Methoxy-L- Arginine, PDB code: 4fvw:
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)-Methoxy-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)-Methoxy-L- Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:30.5 occ:1.00 FE A:HEM801 0.0 30.5 1.0 NA A:HEM801 2.0 33.0 1.0 NC A:HEM801 2.0 27.7 1.0 ND A:HEM801 2.1 33.0 1.0 NB A:HEM801 2.1 33.1 1.0 SG A:CYS415 2.4 30.0 1.0 C4C A:HEM801 3.0 28.3 1.0 C1D A:HEM801 3.1 29.9 1.0 C4A A:HEM801 3.1 32.8 1.0 C1A A:HEM801 3.1 30.9 1.0 C1C A:HEM801 3.1 29.7 1.0 C4B A:HEM801 3.1 31.0 1.0 C1B A:HEM801 3.1 32.2 1.0 C4D A:HEM801 3.2 32.5 1.0 CHD A:HEM801 3.4 30.2 1.0 CB A:CYS415 3.4 29.1 1.0 CHB A:HEM801 3.5 30.5 1.0 CHC A:HEM801 3.5 31.7 1.0 CHA A:HEM801 3.6 31.7 1.0 NH1 A:1KJ803 3.9 49.2 1.0 CA A:CYS415 4.2 26.8 1.0 C3C A:HEM801 4.4 29.1 1.0 NE1 A:TRP409 4.4 31.8 1.0 C3A A:HEM801 4.4 31.7 1.0 C2A A:HEM801 4.4 31.0 1.0 C2D A:HEM801 4.4 31.8 1.0 C2C A:HEM801 4.4 30.6 1.0 C3B A:HEM801 4.4 34.5 1.0 C3D A:HEM801 4.4 33.5 1.0 C2B A:HEM801 4.5 32.7 1.0 C1 A:1KJ803 4.6 47.7 0.3 OH A:1KJ803 4.7 49.8 1.0 CZ A:1KJ803 4.7 41.9 1.0 C1 A:1KJ803 4.8 50.8 0.7 N A:GLY417 4.8 31.3 1.0 C A:CYS415 4.9 30.7 1.0 CD1 A:TRP409 5.0 29.2 1.0

Iron binding site 2 out of 2 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methoxy-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)-Methoxy-L- Arginine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:29.9 occ:1.00 FE B:HEM801 0.0 29.9 1.0 NC B:HEM801 2.0 27.7 1.0 NA B:HEM801 2.0 33.0 1.0 NB B:HEM801 2.1 31.1 1.0 ND B:HEM801 2.1 30.4 1.0 SG B:CYS415 2.4 28.0 1.0 C4C B:HEM801 3.0 26.9 1.0 C1D B:HEM801 3.0 30.1 1.0 C4B B:HEM801 3.1 31.4 1.0 C1A B:HEM801 3.1 28.5 1.0 C4D B:HEM801 3.1 29.6 1.0 C1C B:HEM801 3.1 26.4 1.0 C1B B:HEM801 3.1 31.3 1.0 C4A B:HEM801 3.1 31.0 1.0 CHD B:HEM801 3.4 30.2 1.0 CB B:CYS415 3.4 25.1 1.0 CHC B:HEM801 3.5 28.5 1.0 CHA B:HEM801 3.5 28.4 1.0 CHB B:HEM801 3.5 30.5 1.0 NH1 B:1KJ803 3.9 44.0 1.0 CA B:CYS415 4.2 26.4 1.0 C3C B:HEM801 4.3 28.3 1.0 C2D B:HEM801 4.4 30.1 1.0 C3B B:HEM801 4.4 34.5 1.0 C2C B:HEM801 4.4 27.8 1.0 C2A B:HEM801 4.4 30.7 1.0 C3D B:HEM801 4.4 30.4 1.0 C3A B:HEM801 4.4 30.5 1.0 NE1 B:TRP409 4.4 28.4 1.0 C2B B:HEM801 4.4 33.8 1.0 C1 B:1KJ803 4.5 45.9 0.3 CZ B:1KJ803 4.6 38.5 1.0 OH B:1KJ803 4.8 49.7 1.0 N B:GLY417 4.8 28.4 1.0 C B:CYS415 4.9 28.1 1.0 N B:VAL416 5.0 26.9 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