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

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

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methyl- N(Omega)-Methoxy-L-Arginine, PDB code: 4fvz 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)	38.56 / 1.99
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.899, 110.843, 164.493, 90.00, 90.00, 90.00
R / Rfree (%)	20.2 / 24.5

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methyl- 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)-Methyl- N(Omega)-Methoxy-L-Arginine (pdb code 4fvz). 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)-Methyl- N(Omega)-Methoxy-L-Arginine, PDB code: 4fvz:
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)-Methyl- 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)-Methyl- N(Omega)-Methoxy-L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe801 b:38.1 occ:1.00 FE A:HEM801 0.0 38.1 1.0 NC A:HEM801 2.0 39.6 1.0 NA A:HEM801 2.0 38.5 1.0 ND A:HEM801 2.1 38.1 1.0 NB A:HEM801 2.1 37.5 1.0 SG A:CYS415 2.3 40.8 1.0 C4C A:HEM801 3.0 37.5 1.0 C1D A:HEM801 3.0 38.2 1.0 C4A A:HEM801 3.1 36.5 1.0 C4D A:HEM801 3.1 39.0 1.0 C1C A:HEM801 3.1 39.4 1.0 C4B A:HEM801 3.1 40.6 1.0 C1A A:HEM801 3.2 37.8 1.0 C1B A:HEM801 3.2 38.4 1.0 CB A:CYS415 3.3 36.8 1.0 CHD A:HEM801 3.4 38.0 1.0 CHB A:HEM801 3.5 36.2 1.0 CHC A:HEM801 3.5 39.4 1.0 CHA A:HEM801 3.6 38.0 1.0 OH A:4KJ804 4.0 59.9 1.0 CA A:CYS415 4.1 36.8 1.0 NH2 A:4KJ804 4.2 44.7 1.0 C3C A:HEM801 4.3 40.1 1.0 NE1 A:TRP409 4.3 38.5 1.0 C3A A:HEM801 4.4 36.2 1.0 C2D A:HEM801 4.4 37.4 1.0 C2C A:HEM801 4.4 40.1 1.0 C3D A:HEM801 4.4 38.4 1.0 C2A A:HEM801 4.4 38.0 1.0 C3B A:HEM801 4.5 40.1 1.0 C2 A:4KJ804 4.5 38.6 1.0 C2B A:HEM801 4.5 38.8 1.0 CZ A:4KJ804 4.7 46.3 1.0 N A:GLY417 4.8 38.6 1.0 C A:CYS415 4.8 38.3 1.0 CD1 A:TRP409 4.9 38.3 1.0 N A:VAL416 5.0 38.1 1.0

Iron binding site 2 out of 2 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Methyl- 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)-Methyl- N(Omega)-Methoxy-L-Arginine within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe801 b:33.5 occ:1.00 FE B:HEM801 0.0 33.5 1.0 NC B:HEM801 2.0 36.1 1.0 NA B:HEM801 2.0 37.9 1.0 ND B:HEM801 2.1 36.4 1.0 NB B:HEM801 2.1 37.1 1.0 SG B:CYS415 2.3 30.8 1.0 C4C B:HEM801 3.0 35.6 1.0 C1A B:HEM801 3.1 33.3 1.0 C1D B:HEM801 3.1 37.2 1.0 C4A B:HEM801 3.1 34.9 1.0 C1C B:HEM801 3.1 34.6 1.0 C4D B:HEM801 3.1 35.1 1.0 C4B B:HEM801 3.2 40.0 1.0 C1B B:HEM801 3.2 40.0 1.0 CB B:CYS415 3.3 31.8 1.0 CHD B:HEM801 3.4 36.1 1.0 CHB B:HEM801 3.5 37.8 1.0 CHA B:HEM801 3.5 33.9 1.0 CHC B:HEM801 3.5 38.0 1.0 OH B:4KJ803 3.7 65.9 1.0 CA B:CYS415 4.0 33.7 1.0 NH2 B:4KJ803 4.2 48.8 1.0 C3C B:HEM801 4.3 36.1 1.0 C2A B:HEM801 4.3 35.6 1.0 C3A B:HEM801 4.4 34.2 1.0 NE1 B:TRP409 4.4 38.5 1.0 C2C B:HEM801 4.4 36.2 1.0 C2D B:HEM801 4.4 37.1 1.0 C3D B:HEM801 4.5 37.3 1.0 C3B B:HEM801 4.5 40.7 1.0 C2B B:HEM801 4.5 40.6 1.0 CZ B:4KJ803 4.7 48.0 1.0 N B:GLY417 4.7 39.2 1.0 C B:CYS415 4.8 35.0 1.0 C2 B:4KJ803 4.8 45.3 1.0 N B:VAL416 4.9 36.1 1.0 C1 B:4KJ803 4.9 61.1 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