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Zinc in PDB 6en5: Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
Enzymatic activity of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
All present enzymatic activity of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.:
3.4.15.1;
3.4.15.1;
Protein crystallography data
The structure of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor., PDB code: 6en5
was solved by
G.E.Cozier,
K.R.Acharya,
S.Fienberg,
K.Chibale,
E.D.Sturrock,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
| Resolution Low / High (Å) | 79.48 / 1.75 |
| Space group | P 1 |
| Cell size a, b, c (Å), α, β, γ (°) | 74.167, 103.447, 115.446, 84.86, 85.49, 81.99 |
| R / Rfree (%) | 17.3 / 19.8 |
Other elements in 6en5:
The structure of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor. also contains other interesting chemical elements:
| Magnesium | (Mg) | 4 atoms |
| Chlorine | (Cl) | 4 atoms |
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
(pdb code 6en5). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor., PDB code: 6en5:
Jump to Zinc binding site number: 1; 2; 3; 4;
In total 4 binding sites of Zinc where determined in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor., PDB code: 6en5:
Jump to Zinc binding site number: 1; 2; 3; 4;
Zinc binding site 1 out of 4 in 6en5
Go back to
Zinc Binding Sites List in 6en5
Zinc binding site 1 out
of 4 in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 1 of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor. within 5.0Å range:
|
Zinc binding site 2 out of 4 in 6en5
Go back to
Zinc Binding Sites List in 6en5
Zinc binding site 2 out
of 4 in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 2 of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor. within 5.0Å range:
|
Zinc binding site 3 out of 4 in 6en5
Go back to
Zinc Binding Sites List in 6en5
Zinc binding site 3 out
of 4 in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 3 of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor. within 5.0Å range:
|
Zinc binding site 4 out of 4 in 6en5
Go back to
Zinc Binding Sites List in 6en5
Zinc binding site 4 out
of 4 in the Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor.
Mono view
Stereo pair view
Mono view
Stereo pair view
A full contact list of Zinc with other atoms in the Zn binding
site number 4 of Crystal Structure A of the Angiotensin-1 Converting Enzyme N-Domain in Complex with A Diprolyl Inhibitor. within 5.0Å range:
|
Reference:
S.Fienberg,
G.E.Cozier,
K.R.Acharya,
K.Chibale,
E.D.Sturrock.
The Design and Development of A Potent and Selective Novel Diprolyl Derivative That Binds to the N-Domain of Angiotensin-I Converting Enzyme. J. Med. Chem. V. 61 344 2018.
ISSN: ISSN 1520-4804
PubMed: 29206036
DOI: 10.1021/ACS.JMEDCHEM.7B01478
Page generated: Mon Oct 28 20:12:04 2024
ISSN: ISSN 1520-4804
PubMed: 29206036
DOI: 10.1021/ACS.JMEDCHEM.7B01478
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