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Zinc in PDB 1zzu: Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound

Enzymatic activity of Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound

All present enzymatic activity of Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound:
1.14.13.39;

Protein crystallography data

The structure of Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound, PDB code: 1zzu was solved by H.Li, M.L.Flinspach, J.Igarashi, J.Jamal, W.Yang, J.A.Gomez-Vidal, E.A.Litzinger, R.B.Silverman, T.L.Poulos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 49.91 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.360, 111.130, 165.160, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 22.8

Other elements in 1zzu:

The structure of Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound (pdb code 1zzu). 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 D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound, PDB code: 1zzu:

Zinc binding site 1 out of 1 in 1zzu

Go back to Zinc Binding Sites List in 1zzu
Zinc binding site 1 out of 1 in the Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound


Mono view


Stereo pair view

A full contact list of Zinc with other atoms in the Zn binding site number 1 of Rat Nnos D597N/M336V Double Mutant with L-N(Omega)-Nitroarginine-2,4- L-Diaminobutyric Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:19.2
occ:1.00
 SG A:CYS326 2.3 23.0 1.0
SG B:CYS326 2.3 22.0 1.0
SG A:CYS331 2.3 19.1 1.0
SG B:CYS331 2.3 18.9 1.0
CB A:CYS331 3.3 21.5 1.0
CB B:CYS331 3.3 21.4 1.0
CB B:CYS326 3.4 27.4 1.0
CB A:CYS326 3.5 28.9 1.0
CA A:CYS331 3.6 22.4 1.0
CA B:CYS331 3.6 22.0 1.0
N A:MET332 4.0 22.2 1.0
N B:MET332 4.0 20.6 1.0
N A:GLY333 4.2 20.4 1.0
C A:CYS331 4.2 22.3 1.0
N B:GLY333 4.2 19.3 1.0
C B:CYS331 4.2 21.4 1.0
CA A:GLY333 4.6 20.0 1.0
CA B:GLY333 4.6 20.4 1.0
O A:HOH1069 4.8 33.8 1.0
CA B:CYS326 4.8 28.5 1.0
N A:CYS331 4.9 23.8 1.0
CA A:CYS326 4.9 30.8 1.0
N B:CYS331 4.9 24.1 1.0
O B:ILE330 5.0 26.6 1.0
C A:MET332 5.0 21.8 1.0

Reference:

H.Li, M.L.Flinspach, J.Igarashi, J.Jamal, W.Yang, E.A.Litzinger, H.Huang, E.P.Erdal, R.B.Silverman, T.L.Poulos. Exploring the Binding Conformations of Bulkier Dipeptide Amide Inhibitors in Constitutive Nitric Oxide Synthases. Biochemistry V. 44 15222 2005.
ISSN: ISSN 0006-2960
PubMed: 16285725
DOI: 10.1021/BI0513610
Page generated: Wed Oct 16 21:27:52 2024

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