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Iron in PDB 1qw6: Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg.

Enzymatic activity of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg.

All present enzymatic activity of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg.:
1.14.13.39;

Protein crystallography data

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg., PDB code: 1qw6 was solved by R.Fedorov, E.Hartmann, 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 / 2.10
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 45.004, 108.899, 164.767, 90.00, 90.00, 90.00
R / Rfree (%) 19.5 / 24.3

Other elements in 1qw6:

The structure of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg. also contains other interesting chemical elements:

Zinc (Zn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg. (pdb code 1qw6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg., PDB code: 1qw6:

Iron binding site 1 out of 1 in 1qw6

Go back to Iron Binding Sites List in 1qw6
Iron binding site 1 out of 1 in the Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg.


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Rat Neuronal Nitric Oxide Synthase Oxygenase Domain in Complex with N- Omega-Propyl-L-Arg. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe900

b:18.2
occ:1.00
 FE A:HEM900 0.0 18.2 1.0
NA A:HEM900 2.0 23.8 1.0
ND A:HEM900 2.0 22.9 1.0
NB A:HEM900 2.0 19.7 1.0
NC A:HEM900 2.0 26.5 1.0
SG A:CYS415 2.2 19.5 1.0
C4A A:HEM900 3.0 14.9 1.0
C1D A:HEM900 3.1 22.9 1.0
C1B A:HEM900 3.1 24.6 1.0
C1A A:HEM900 3.1 19.6 1.0
C4D A:HEM900 3.1 19.4 1.0
C4C A:HEM900 3.1 23.0 1.0
C4B A:HEM900 3.1 26.2 1.0
C1C A:HEM900 3.1 24.1 1.0
CB A:CYS415 3.4 15.1 1.0
CHB A:HEM900 3.4 21.2 1.0
CHD A:HEM900 3.4 16.1 1.0
CHA A:HEM900 3.5 20.1 1.0
CHC A:HEM900 3.5 23.8 1.0
O A:HOH82 3.5 29.9 1.0
C1 A:3AR902 4.0 27.9 1.0
CA A:CYS415 4.1 15.7 1.0
C3A A:HEM900 4.3 26.3 1.0
C2D A:HEM900 4.3 21.1 1.0
C2A A:HEM900 4.3 25.1 1.0
C3D A:HEM900 4.3 19.6 1.0
C2B A:HEM900 4.3 25.3 1.0
C3B A:HEM900 4.3 26.7 1.0
C3C A:HEM900 4.4 25.6 1.0
C2C A:HEM900 4.4 24.0 1.0
NE1 A:TRP409 4.5 19.8 1.0
NH1 A:3AR902 4.8 29.2 1.0
C A:CYS415 4.8 13.9 1.0
N A:GLY417 4.8 15.6 1.0
CZ A:3AR902 4.9 27.7 1.0
N A:VAL416 4.9 17.0 1.0

Reference:

R.Fedorov, E.Hartmann, D.K.Ghosh, I.Schlichting. Structural Basis For the Specificity of the Nitric-Oxide Synthase Inhibitors W1400 and Nomega-Propyl-L-Arg For the Inducible and Neuronal Isoforms. J.Biol.Chem. V. 278 45818 2003.
ISSN: ISSN 0021-9258
PubMed: 12954642
DOI: 10.1074/JBC.M306030200
Page generated: Wed Jul 16 20:09:18 2025

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