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Chlorine in PDB 4x8i: De Novo Crystal Structure of the Pyrococcus Furiosus TET3 AminopeptidaseEnzymatic activity of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase
All present enzymatic activity of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase:
3.4.11.15; Protein crystallography data
The structure of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase, PDB code: 4x8i
was solved by
M.Colombo,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4x8i:
The structure of De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase
(pdb code 4x8i). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 3 binding sites of Chlorine where determined in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase, PDB code: 4x8i: Jump to Chlorine binding site number: 1; 2; 3; Chlorine binding site 1 out of 3 in 4x8iGo back to![]() ![]()
Chlorine binding site 1 out
of 3 in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase
![]() Mono view ![]() Stereo pair view
Chlorine binding site 2 out of 3 in 4x8iGo back to![]() ![]()
Chlorine binding site 2 out
of 3 in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase
![]() Mono view ![]() Stereo pair view
Chlorine binding site 3 out of 3 in 4x8iGo back to![]() ![]()
Chlorine binding site 3 out
of 3 in the De Novo Crystal Structure of the Pyrococcus Furiosus TET3 Aminopeptidase
![]() Mono view ![]() Stereo pair view
Reference:
M.Colombo,
E.Girard,
B.Franzetti.
Tuned By Metals: the Tet Peptidase Activity Is Controlled By 3 Metal Binding Sites. Sci Rep V. 6 20876 2016.
Page generated: Sat Dec 12 11:19:51 2020
ISSN: ESSN 2045-2322 PubMed: 26853450 DOI: 10.1038/SREP20876 |
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