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Zinc in PDB 1p6j: Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound

Enzymatic activity of Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound

All present enzymatic activity of Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound:
1.14.13.39;

Protein crystallography data

The structure of Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound, PDB code: 1p6j was solved by M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.-M.Hah, 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) 46.04 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 52.330, 111.050, 164.690, 90.00, 90.00, 90.00
R / Rfree (%) 22.5 / 25.9

Other elements in 1p6j:

The structure of Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound also contains other interesting chemical elements:

Iron (Fe) 2 atoms

Zinc Binding Sites:

The binding sites of Zinc atom in the Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound (pdb code 1p6j). 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 Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound, PDB code: 1p6j:

Zinc binding site 1 out of 1 in 1p6j

Go back to Zinc Binding Sites List in 1p6j
Zinc binding site 1 out of 1 in the Rat Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline 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 Neuronal Nos Heme Domain with L-N(Omega)-Nitroarginine-(4R)-Amino- L-Proline Amide Bound within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Zn900

b:36.0
occ:1.00
SG A:CYS326 2.3 41.2 1.0
SG B:CYS331 2.3 38.6 1.0
SG A:CYS331 2.3 38.6 1.0
SG B:CYS326 2.3 40.0 1.0
CB B:CYS331 3.3 41.0 1.0
CB A:CYS331 3.3 41.5 1.0
CB A:CYS326 3.4 46.9 1.0
CB B:CYS326 3.5 45.5 1.0
CA B:CYS331 3.6 41.1 1.0
CA A:CYS331 3.6 41.9 1.0
N A:MET332 4.0 41.4 1.0
N B:MET332 4.1 40.7 1.0
N A:GLY333 4.1 40.4 1.0
C A:CYS331 4.2 41.6 1.0
N B:GLY333 4.2 39.4 1.0
C B:CYS331 4.3 40.8 1.0
CA A:GLY333 4.5 39.8 1.0
CA B:GLY333 4.6 39.1 1.0
CA A:CYS326 4.8 48.1 1.0
N B:CYS331 4.9 42.5 1.0
N A:CYS331 4.9 43.3 1.0
CA B:CYS326 4.9 46.5 1.0
C A:MET332 4.9 41.1 1.0

Reference:

M.L.Flinspach, H.Li, J.Jamal, W.Yang, H.Huang, J.M.Hah, J.A.Gomez-Vidal, E.A.Litzinger, R.B.Silverman, T.L.Poulos. Structural Basis For Dipeptide Amide Isoform-Selective Inhibition of Neuronal Nitric Oxide Synthase. Nat.Struct.Mol.Biol. V. 11 54 2004.
ISSN: ISSN 1545-9993
PubMed: 14718923
DOI: 10.1038/NSMB704
Page generated: Wed Dec 16 03:00:31 2020

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