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Chlorine in PDB 4ufa: Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-SdEnzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd
All present enzymatic activity of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd:
3.4.15.1; Protein crystallography data
The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd, PDB code: 4ufa
was solved by
G.Masuyer,
R.G.Douglas,
E.D.Sturrock,
K.R.Acharya,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4ufa:
The structure of Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd
(pdb code 4ufa). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd, PDB code: 4ufa: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 4ufaGo back to Chlorine Binding Sites List in 4ufa
Chlorine binding site 1 out
of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 4ufaGo back to Chlorine Binding Sites List in 4ufa
Chlorine binding site 2 out
of 2 in the Crystal Structure of the Angiotensin-1 Converting Enzyme N- Domain in Complex with Ac-Sd
Mono view Stereo pair view
Reference:
G.Masuyer,
R.G.Douglas,
E.D.Sturrock,
K.R.Acharya.
Structural Basis of Ac-Sdkp Hydrolysis By Angiotensin-I Converting Enzyme Sci.Rep. V. 5 13742 2015.
Page generated: Sat Dec 12 11:15:06 2020
ISSN: ISSN 2045-2322 PubMed: 26403559 DOI: 10.1038/SREP13742 |
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