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Atomistry » Zinc » PDB 4ggg-4gsk » 4gqe » |
Zinc in PDB 4gqe: Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-NorvalineEnzymatic activity of Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline
All present enzymatic activity of Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline:
1.14.13.39; Protein crystallography data
The structure of Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline, PDB code: 4gqe
was solved by
H.Li,
T.L.Poulos,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4gqe:
The structure of Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline
(pdb code 4gqe). 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 Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline, PDB code: 4gqe: Zinc binding site 1 out of 1 in 4gqeGo back to Zinc Binding Sites List in 4gqe
Zinc binding site 1 out
of 1 in the Structure of Rat Neuronal Nitric Oxide Synthase Heme Domain in Complex with (5E)-5-[(N-Tert-Butoxycarbamimidoyl)Imino]-L-Norvaline
Mono view Stereo pair view
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.
Page generated: Sat Oct 26 23:25:12 2024
ISSN: ISSN 0006-2960 PubMed: 23586781 DOI: 10.1021/BI301571V |
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