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

Enzymatic activity of 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;

Protein crystallography data

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

Other elements in 2hx4:

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:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc 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 Zinc atom.
In total only one binding site of Zinc was determined in the Rat Nnos Heme Domain Complexed with 4-N-(Nw-Nitro-L-Argininyl)-Trans- 4-Hydroxyamino-L-Proline Amide, PDB code: 2hx4:

Zinc binding site 1 out of 1 in 2hx4

Go back to Zinc Binding Sites List in 2hx4
Zinc binding site 1 out of 1 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 Zinc with other atoms in the Zn 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:Zn900

b:30.0
occ:1.00
 SG A:CYS326 2.3 35.8 1.0
SG B:CYS326 2.3 33.1 1.0
SG A:CYS331 2.3 27.6 1.0
SG B:CYS331 2.4 30.8 1.0
CB A:CYS331 3.2 32.9 1.0
CB B:CYS331 3.3 36.4 1.0
CB A:CYS326 3.3 40.4 1.0
CA A:CYS331 3.5 34.5 1.0
CB B:CYS326 3.6 39.9 1.0
CA B:CYS331 3.6 35.7 1.0
N A:MET332 4.0 33.2 1.0
N B:MET332 4.1 32.3 1.0
N A:GLY333 4.1 33.4 1.0
C A:CYS331 4.2 33.5 1.0
N B:GLY333 4.2 28.8 1.0
C B:CYS331 4.2 34.2 1.0
CA A:GLY333 4.5 31.4 1.0
CA B:GLY333 4.6 28.7 1.0
CA A:CYS326 4.8 42.6 1.0
N A:CYS331 4.8 37.5 1.0
N B:CYS331 4.8 39.7 1.0
O B:ILE330 4.9 42.1 1.0
CA B:CYS326 5.0 43.5 1.0
C A:MET332 5.0 33.8 1.0
O A:HOH963 5.0 36.6 1.0

Reference:

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
Page generated: Thu Oct 17 00:44:38 2024

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