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Zinc in PDB 4fvx: Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine

Enzymatic activity of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine

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

Protein crystallography data

The structure of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine, PDB code: 4fvx 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) 37.80 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.000, 111.280, 165.120, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 22.1

Other elements in 4fvx:

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

Fluorine (F) 6 atoms
Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine (pdb code 4fvx). 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 Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine, PDB code: 4fvx:

Zinc binding site 1 out of 1 in 4fvx

Go back to Zinc Binding Sites List in 4fvx
Zinc binding site 1 out of 1 in the Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Structure of Rat Nnos Heme Domain in Complex with N(Omega)-Ethoxy-L- Arginine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn805

b:37.6
occ:1.00
 SG A:CYS326 2.4 45.0 1.0
SG A:CYS331 2.4 37.4 1.0
SG B:CYS326 2.4 41.3 1.0
SG B:CYS331 2.4 37.9 1.0
CB B:CYS331 3.2 42.0 1.0
CB A:CYS331 3.3 41.0 1.0
CB A:CYS326 3.4 50.8 1.0
CB B:CYS326 3.5 48.9 1.0
CA A:CYS331 3.6 44.0 1.0
CA B:CYS331 3.6 42.1 1.0
N A:MET332 3.9 43.5 1.0
N A:GLY333 4.1 39.9 1.0
N B:MET332 4.1 39.3 1.0
C A:CYS331 4.2 43.6 1.0
N B:GLY333 4.3 37.1 1.0
C B:CYS331 4.3 40.6 1.0
CA A:GLY333 4.6 38.1 1.0
CA B:GLY333 4.7 35.4 1.0
CA A:CYS326 4.8 52.9 1.0
O A:HOH1027 4.8 46.0 1.0
N A:CYS331 4.9 46.9 1.0
CA B:CYS326 4.9 50.4 1.0
N B:CYS331 4.9 44.8 1.0
C A:MET332 4.9 41.1 1.0
CA A:MET332 5.0 43.5 1.0

Reference:

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
Page generated: Sat Oct 26 22:57:57 2024

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