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Zinc in PDB 6av7: Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69Enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69
All present enzymatic activity of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69:
1.14.13.39; Protein crystallography data
The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69, PDB code: 6av7
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 6av7:
The structure of Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69
(pdb code 6av7). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69, PDB code: 6av7: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 6av7Go back to Zinc Binding Sites List in 6av7
Zinc binding site 1 out
of 2 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 6av7Go back to Zinc Binding Sites List in 6av7
Zinc binding site 2 out
of 2 in the Structure of Human Endothelial Nitric Oxide Synthase Heme Domain in Complex with HW69
Mono view Stereo pair view
Reference:
H.T.Do,
H.Y.Wang,
H.Li,
G.Chreifi,
T.L.Poulos,
R.B.Silverman.
Improvement of Cell Permeability of Human Neuronal Nitric Oxide Synthase Inhibitors Using Potent and Selective 2-Aminopyridine-Based Scaffolds with A Fluorobenzene Linker. J. Med. Chem. V. 60 9360 2017.
Page generated: Wed Dec 16 11:30:54 2020
ISSN: ISSN 1520-4804 PubMed: 29091437 DOI: 10.1021/ACS.JMEDCHEM.7B01356 |
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